PT851934E - Plantas que sintetizam um amido modificado, processo para a sua produção e amido modificado - Google Patents
Plantas que sintetizam um amido modificado, processo para a sua produção e amido modificado Download PDFInfo
- Publication number
- PT851934E PT851934E PT96932575T PT96932575T PT851934E PT 851934 E PT851934 E PT 851934E PT 96932575 T PT96932575 T PT 96932575T PT 96932575 T PT96932575 T PT 96932575T PT 851934 E PT851934 E PT 851934E
- Authority
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- Prior art keywords
- leu
- glu
- ser
- asp
- ala
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- 239000004368 Modified starch Substances 0.000 title 2
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- WBPFYNYTYASCQP-CYDGBPFRSA-N Val-Val-Ile Chemical compound CC[C@H](C)[C@@H](C(=O)O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C(C)C)N WBPFYNYTYASCQP-CYDGBPFRSA-N 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 108010056243 alanylalanine Proteins 0.000 description 1
- 108010070944 alanylhistidine Proteins 0.000 description 1
- ZVDPYSVOZFINEE-BQBZGAKWSA-N alpha-Asp-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@@H](N)CC(O)=O ZVDPYSVOZFINEE-BQBZGAKWSA-N 0.000 description 1
- 108010050025 alpha-glutamyltryptophan Proteins 0.000 description 1
- 108010008355 arginyl-glutamine Proteins 0.000 description 1
- 108010052670 arginyl-glutamyl-glutamic acid Proteins 0.000 description 1
- 108010072041 arginyl-glycyl-aspartic acid Proteins 0.000 description 1
- 108010091092 arginyl-glycyl-proline Proteins 0.000 description 1
- 108010029539 arginyl-prolyl-proline Proteins 0.000 description 1
- 108010062796 arginyllysine Proteins 0.000 description 1
- 108010060035 arginylproline Proteins 0.000 description 1
- 108010077245 asparaginyl-proline Proteins 0.000 description 1
- 108010092854 aspartyllysine Proteins 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 108010063718 gamma-glutamylaspartic acid Proteins 0.000 description 1
- 108010080575 glutamyl-aspartyl-alanine Proteins 0.000 description 1
- VPZXBVLAVMBEQI-UHFFFAOYSA-N glycyl-DL-alpha-alanine Natural products OC(=O)C(C)NC(=O)CN VPZXBVLAVMBEQI-UHFFFAOYSA-N 0.000 description 1
- 108010040030 histidinoalanine Proteins 0.000 description 1
- 108010028295 histidylhistidine Proteins 0.000 description 1
- 108010085325 histidylproline Proteins 0.000 description 1
- 108010018006 histidylserine Proteins 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- DVCSNHXRZUVYAM-BQBZGAKWSA-N leu-asp Chemical compound CC(C)C[C@H](N)C(=O)N[C@H](C(O)=O)CC(O)=O DVCSNHXRZUVYAM-BQBZGAKWSA-N 0.000 description 1
- 108010077158 leucinyl-arginyl-tryptophan Proteins 0.000 description 1
- 108010034529 leucyl-lysine Proteins 0.000 description 1
- 108010090333 leucyl-lysyl-proline Proteins 0.000 description 1
- 108010073472 leucyl-prolyl-proline Proteins 0.000 description 1
- 108010000761 leucylarginine Proteins 0.000 description 1
- 108010009298 lysylglutamic acid Proteins 0.000 description 1
- 108010064235 lysylglycine Proteins 0.000 description 1
- 108010054155 lysyllysine Proteins 0.000 description 1
- 108010056582 methionylglutamic acid Proteins 0.000 description 1
- OKSCSVIOPIVWTC-KRWDZBQOSA-N methyl (2s)-2-[[2-[4-[bis(2-chloroethyl)amino]phenyl]acetyl]amino]-3-(1h-imidazol-5-yl)propanoate Chemical compound C([C@@H](C(=O)OC)NC(=O)CC=1C=CC(=CC=1)N(CCCl)CCCl)C1=CN=CN1 OKSCSVIOPIVWTC-KRWDZBQOSA-N 0.000 description 1
- 210000004498 neuroglial cell Anatomy 0.000 description 1
- 108010077112 prolyl-proline Proteins 0.000 description 1
- 102220040233 rs79219465 Human genes 0.000 description 1
- 108010071207 serylmethionine Proteins 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 108010020532 tyrosyl-proline Proteins 0.000 description 1
- 108010078580 tyrosylleucine Proteins 0.000 description 1
- IBIDRSSEHFLGSD-UHFFFAOYSA-N valinyl-arginine Natural products CC(C)C(N)C(=O)NC(C(O)=O)CCCN=C(N)N IBIDRSSEHFLGSD-UHFFFAOYSA-N 0.000 description 1
Classifications
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/415—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from plants
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23B—PRESERVATION OF FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES; CHEMICAL RIPENING OF FRUIT OR VEGETABLES
- A23B7/00—Preservation of fruit or vegetables; Chemical ripening of fruit or vegetables
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L19/00—Products from fruits or vegetables; Preparation or treatment thereof
- A23L19/10—Products from fruits or vegetables; Preparation or treatment thereof of tuberous or like starch containing root crops
- A23L19/12—Products from fruits or vegetables; Preparation or treatment thereof of tuberous or like starch containing root crops of potatoes
- A23L19/18—Roasted or fried products, e.g. snacks or chips
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- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08B—POLYSACCHARIDES; DERIVATIVES THEREOF
- C08B30/00—Preparation of starch, degraded or non-chemically modified starch, amylose, or amylopectin
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- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08B—POLYSACCHARIDES; DERIVATIVES THEREOF
- C08B30/00—Preparation of starch, degraded or non-chemically modified starch, amylose, or amylopectin
- C08B30/04—Extraction or purification
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- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
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- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/82—Vectors or expression systems specially adapted for eukaryotic hosts for plant cells, e.g. plant artificial chromosomes (PACs)
- C12N15/8241—Phenotypically and genetically modified plants via recombinant DNA technology
- C12N15/8242—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits
- C12N15/8243—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits involving biosynthetic or metabolic pathways, i.e. metabolic engineering, e.g. nicotine, caffeine
- C12N15/8245—Phenotypically and genetically modified plants via recombinant DNA technology with non-agronomic quality (output) traits, e.g. for industrial processing; Value added, non-agronomic traits involving biosynthetic or metabolic pathways, i.e. metabolic engineering, e.g. nicotine, caffeine involving modified carbohydrate or sugar alcohol metabolism, e.g. starch biosynthesis
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- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
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- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
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- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/10—Transferases (2.)
- C12N9/1048—Glycosyltransferases (2.4)
- C12N9/1051—Hexosyltransferases (2.4.1)
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- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P19/00—Preparation of compounds containing saccharide radicals
- C12P19/04—Polysaccharides, i.e. compounds containing more than five saccharide radicals attached to each other by glycosidic bonds
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- Genetics & Genomics (AREA)
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- General Engineering & Computer Science (AREA)
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- Nutrition Science (AREA)
- Biophysics (AREA)
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- Proteomics, Peptides & Aminoacids (AREA)
- Breeding Of Plants And Reproduction By Means Of Culturing (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Description
DS5CM:ÇJI/0
PlJti-ims QUE SIHTSPIZÃM. GM AMIDO MODIFICADO, PROCS3SSO GAGâ Ã SI» PRODUÇÃO 1 AMIDO MJOXFICGaJGO
be^co· .·.ert u; reseri1.>.rn i·;.ΐe ο ; teehλ' ncpu. OdrViuroroe ' a nirseura reaccional e ceteiirirurj-se a quant:idade de íOIDa por meio da absorção a 340 nm. O teor de qlicose- 6- fosfato por 1 mg de arai do esiá indicado no quadro que se segue para os plantas de
Ui! TIPO DE MOLÉCULA: ADNc 8 ARNm (vi) FONTE ORIGINAL:
ίτ:α ΑΑ, Fer. A ’Α
Leu Tre 7:: TCT GA.G 01 h GCA GAA PAG TTC AAÍ CIA GGG GGG ΑΑΪ ΑΓΊ GAG GTA CAG Ser G.iu Leu Ala Geu Le.s Fen Ser Leu Gj. i Gli Asn JG;..e Giu Leu Gin H ;_i vj cè f> 1 fí\
7 '//7 AnG Ί GG 52.5 A-2G2 A AG LOgOa sAn 1.5 5 25 15 5 5.2 2 22:.52 CGA GA.g iííg: ir-ÍAG' 7 Leu Ar T Trp 5], u Ar g L.i s Gl: Lis 5:' 1 As 5 Tir 15' O Fro Giu Lis Clu 2 5 0 555 24 0 A AG G53 GAA 5A'r GAG Ga 3 ‘1. GCT CGA 152 Ϊ GTG C12A GAG siriS GA/i ATA GCT Li 3 GAu G i u T i r 5.1. u AI. 3 Ai 3 A.rg Tre Võ.l Gen Gin Glu Glu Γ1« Ala 55 2 45 5 2 60 CGT GGT GCT TCC ATA CAG GAC ATT CG A GC A AGG CTA ACA AAA ACT AAT 932 Trg G.Li íU a Ser Ile Gin Asp Ile .Ar ·.:· Ala Arg Leu Tre Lis Tre Asn 265 2 7 0 275 GA Τ' AAA AG T CAA AGC AAA ΆΑΑ GAG GCT CGT r · r GTA ACA AAG AGT GAT 910 ÃSp IA 9 Ser Gin Ser Lis G1 u Gi u Pro 7e li iT i- G Vai Tre Lis Ser Asp 280 ΆΆ 290 ΑΤΆ CCT GAT GAC CTT GCC CAA GCA CAA GCT 1AC ATT AGG TGG GA.G AAA ± ie r- Asp Asp leri Ala Gin AI a Glr: õ. 'T r Ile Arg Trp Glu Lis 2 95 300 305 GCA Άτ’οΑό. AAG CCG AAC TAT CCT CCA GAA GAG CAA ATT GAA GAA CTC GAA 1 0 7 6 P.1,3 G1 í 1. i κ Pro Asn Tir Pro Pro G1 u Lis G 1 Γ: lie Glu Glu Leu Glu 310 315 320 GAA GCA AGA AGA GAA TTG CAA CTT GAG CTT CAG AAA GGC ATT ACC CTT 1124 G X G Ala Ar q Arg Glu Leu G.l n Leu Clu f... i G1 Li L is Gli Ile Tre Leu 325 330 2 35 310 GAT GA.G TTG CGG AAA ACG ATT ACA AAA GGG GAG ATA AAA ACT AAG GTG 1.17 2 Asp Glu Leu Ar g Lis Tie Ila '1 re Lis Gli Glu lie 1 i S Tre Lia Vai 34 3 350 355 GAA AAG CAC CTG AAA AGA AGI TCT TTT GCC GTT GAA AGA ATC CAA A.e, r\ 1220 G1 u Lis Kis Leu Lis Arq Ser Ser Fen Ala Vai Glr Arg ile Gin Arg 360 365 3?0 AAG AAící AGA GAC TTT ipí g; ,g- CAT CTT ATT AAT AAG TAT ACT TCC AGT CCT 12 68 Lis Lis Ara Asp Fe λ G .1 i iíis Leu Ile Asn Lis Tir Tre Ser Ser Pro 37 3 280 38 5 uC A GTA CAA GTA Cl A; PAG GTC TTG GAA GAA CCA CCA GCC TTA TCT 1316 Ala Vai Gin Vai G2 n Lr s Vai Glu Glu Pro Pre Aj :-í Leu Ser li 3 90 395 400 ATT AAC CTG TAT GCC AAG GAG AAG GAG GAG CAG ATT GAT GAT CCG ATC 1364 Ile Lis Leu Tir Ala Lis Glu Lis Glu Glu Gin Ile Asp A.sp Pre Ile 405 410 415 420 CTA AAT AAA AAG ATC TTT AAG GTC GAT GAT GGG GAG CTA CTG GTA CTG 1412 75 lie Feη 4 25
GTA GCA AAG TCT AAG ACA AAA Vai Ais Lis S r Ser •p .1. L1. s ire Lis 4 4 C 215 AAT CAG CCA .ATT .ACT CT1 CAC TGG GCA Asn Gin Fr o Ile Tra I.su lis Ί0'·Ρ Ala 4 55 5 60 TGG ATG GTA CCA CCi TCP. AAG ATA TTG Trp Met Vai Pr o Prc S e r S e r: Ile Leu 470 4/5 GAC AAG GCC '—-5' Àj ACA CCi' TCT TCA Asp Lis Ala Alt, Gi. α Tre F r o E'en Ser 4 85 4 90 ACT TCT AAG GTA CAA TCT TTG GAT ATA Ti e Ser L í 8 Vai Gin Ser Leu Asp Ile 505 GTG GtA ATG CCA TTT GTT GTT TTG TCT Vai Gli Met Pr o Fen vai Leu Le u Ser 520 : o r, GAA GGG ICC GAT TTC TAT GTT GGC TTC Gin Gli Ser Asp Fen TAr Va.l Gli Fen 535 54 0 O O AAG GCT GCT GGG GAT GGC AGT GGA Leu Lis Ala Ala Gli Asp Gli Ser Gli 550 555 AAA ATA GCA GAT ATG GAA AGT GAG GCT
Asp Gli Gxu Leu Leu \'al Leu 430 4 35 GTA CAT CTA GCT hCA GAT CTG 14 60 Vai His Leu Ala ' [’ Τ' A; Asp Leu 150 TTA TCC AAA AGT CCT GGA GAG ; 508 Leu Ser Lis Ser Prc. Gli Glu 466 CCT CCT GGG TCA ATT ATT TTA 1556 Prc Pro Gli Ser Tie Ile Leu 480 ccc AGT TCT TCT GAT GGT CTA 1604 Ala Ser Ser Ser Asp Gli Leu 495 500 GTA ATT GAA GAT GGC AAT TTT 1 652 vai Ile Glu Asp Gli Asn Fen 53 0 515 GGT G.AA AAA TGG ATT AA.G AAC 1700 G1 i Glu Lík Trp lie Lis Asn 530 AGT GCT GCA TCC níci TTA GCA 3748 Ser Ala Ala Ser I. .l s Leu. Ala 545 ACT GCA AAG TCT TTA CTG GAT 1796 Tre Ala Lis Ser Leu Leu Asp 560 CAG AAG TCA TTT ATG CAC CGG 1844
Lis Ile Ala Asp Met alu Ser Glu Ala Gin Lis Ser Fen Met His Arg 565 570 575 580 TTT AAT ATT GCA GCT GAC TTG ATA GAA GAT GCC ACT AGT GCT GGT GAA 1892 Fen Asn Ile Ala Ala Asp Leu Ile Glu Asp Ala Tre Ser Ala Gli Glu 76 CT? ml TTT CGT GGA r :w CTT GT.A TGG ATG AGG 7TC ATG GCT ACA. AGG .1 9 4 C Leu G1> E'en Ala G.Li Ile Le α Vai Trp Mel: Are; Fen Me t Ala Tt e Arg 600 6 0 5 c i ti CA.A CTG ATA TGG AAC AJA AAC TAT AAC GTA AAA CCA GGT GAA. ATA AGG 195 8 G1 π Leu 11 e Trp Asn Lis Asa T 1 ϊ- A.s n Vai Lis Pro Arg G1 u Ile Ge r 615 6 5 U 625 AAG GCn CAG GAC AGA CTT AGA GAC TTG TTG CAG AAT GCT TTG ACC AGT 2 6 3 6 Lis Ala Gin Asp Lry ,..;cU Tre Asp Leu Leu Gin Asn Ala Feri T r e Ser óuO 635 640 CAC CCT CAG TAC CGT GAA ATT TTG CGG ATG ATT ATG TGA ACT GTT GGA 2 0 8 4 His Pro Gin T..r Arg Glu lie Leu Arg Met Ile Met set Tre Vai G ; 1 645 6 30 65 5 6 o 0 CGT GGA CGT GAA GGG GAT ΰ TA GGA CAG GGA ATT HoU GAT GAA ATT TTG a 15 r Arg C-í 1 i Glx Giu G1 i Asp Vai Gli Gin Arg ile Arg Asp Glu 11 a Leu 665 670 67 5 GTC ATC CAG AGG AAC AAT GAC TGC AAG GGT GGT ATG ATG CAA GAA TGG Lai 11 e GJ n Arg .As ri Asn Asp Cis Lis Gli Gii Mel.. Met GI n Glu Trp 680 685 690 CAT CAG AAA TTG CAT .AAT AAT ACT AGT CCT GAT GAT GTT GTG ATC TGT 2228 His G1 r> Lis Leu Kis Asn Asn Tre Ser £'ro Asp Asp La 1 vai lie Cis 695 100 7 0 5 r Ae GCA ΤΪΑ ATT ΠΑΤΑ,· TAC ATC AAG AGT GAT TTT GAT CTT GGT GTT TAT 22 7 6 G1 n Ala Leu lie Ah pi Tir Ile Lis Ser Asp Feri Asp Le u G1 i vai T i r 710 715 720 TGG AAA ACC CTG AAT GAG AAC GGA ATA ACA AAA GAG CGT CTT TTG AGT 2324 Trp Lis Tre Leu Asn Glu Asn Gli Ile Tre Lis Glu Arg Leu Leu Ser 725 730 735 740 TAT GAC CGT GCT ATC CAT TCT GAA CCA AAT TTT AGA GGA GAT CAA 2372 Tir Asp Arg Ala Ile His Ser Glu Pro Asn Fen Arg Gli Asp Gin Lxs 745 750 755 77 GCT ngo CTT CGT GAT ΤΤΛ GCT GAG TAT ATG AGA AC A TTG m.u GCA .7 4 2 0 ρΊ ; a : ; Le u Leu Arg Ase G 0 i Hl 5 Tir Met Arg Tre Leu Lxs AI ci 7 6 a 765 77 0 GTT (: rr" TCA V m ;; h. J C CT G7LG TCI GC’ T ATT GCA AA( 7; TGi 7 AT( P GGC 24 56 ν,-ί:: Lis Ser C1 1 Ala Asp T.ícU Glu Ser Ala I r e Ala Asn Cis Met Gl i 77 5 "r A. · : 78 7 TAC AAA ACT GAG GGA G .77- G'yC TTT ATG GTT ,:r :·Ί. GTC CAG ATA AAT CC Τ 2516 Tir Lio Ί re G.1 u Gli GJ.u Gli Met Vai Gli. Vai Gin Ile Asn ΡΙΟ 7 9 0 y A 8 00 GTA 7’7'A GGC TTG ;a:a TCI GGC T':p "Γ .·' V. GAC CTC CTC CAT ΤΪΪ GTC TTA 2 5 d 4 Vai Sei G1 í Leu Aro 07 ir CL i Frcn Gin Asp Leu .Leu His Fen Vai Leu 801 610 820 8 2 5 GAC CAT GTG ' -.ióA GAT AAA AAT GT G GAA ACT CTT CTT ./:,1:1: AGA TTG CTA 2612 Asp hl í; uai GA Asp Lis A o u Vai G1 u Tre Leu Leu Gi. U Arg leu Lou cl: 5 630 8 35 GAG GCT CGT GAS GAG CTT AGG ccc TTG CTT CTC AAA CCA AAC AAC CGT 2660 Glu A1 a Arg Glu Glu Leu Arg Pro Leu Leu Leu Lis Oiro Asn Asn Arg 84 0 645 850 CTA AAG GAT CAA CTG TXT TTG 'ci/Hl .ATA GCA CTT GAT TCT ACA GTT AGA. 2703 Leu Lis Asp Leu Leu feri Leu Asp Ile Ala Leu Asp Ser Tre Va.l Arg 855 8 0 0 6 65 ACA GCA G TA GAA AGG GGA TAT GAA GAA TTG AAC AAC GCT AAT GCT GAG 27 56 Tre AI a Vai oi 0. Arg Gli T i r Glu Gi.u Leu Asr: Asa Ala Asn Pro Gl u 8 70 3 7 5 880 AAA ATC ATG TAC TTC ATC TCC CTC GTT CTT GAA AAT CTC GCA CTC TCT 2804 Lis Ile Met Tir Feri Ile Ser Leu Vai Leu Glu Asn Leu Ala Leu Ser 885 890 895 900 GTG GAC GAT AAT GAA GAT CTT GTT TAT TGC TTG AAG GGA TGG AAT CAA 2852 V âi Asp Asp Asp Glu Asp Leu Vai Tir Cis Leu Lis Gli Trp Asn Gin 905 910 915 GCT CTT TCA ATG TCC AAT GGT 00G GAC AAC CAT TGG GCT TTA TTT GCA 2900 78
Ai /: Leu Ser Met Ger Asn G.l i G1. i. Asp Asn His Trp AI a Leo Fen Ala 920 925 93 f ; sj-Λ GCT GTG CTT GAC AGA ACC CGT GTT GCA CTT GCA AG C AAG GCA GAG 2 94 S L.i S Ala vai Leu Asp Arg ’ Arg Leu Ala Leu Ala Γ.7 ·>· T Li s AI a Glu 951 °4 0 94 5 TGG TAC CA! CAC TCA TTG GAG OCA TCT GCC GAA TAT CTA GGA TCA ATA 2 99 6 T rp Tir fí: a His Leu Leu Gin Pr,r Ser Ala Glu Tir Ler G.I i Ser Ile 950 C. r r. 960 CTT GGG GTG GAC CAA TGG GCT TTG AAC ATA TTT ACT GAA GAA ATT ATA 3 044 Leu Gli Vai Asp Gin Trp . 1 ri Leu Asn lie Fen Tre Glu Glu Ile Ile 7 6 5 971 975 980 CGT GCT GGA TCA GOA GCT TTG. TCC TCT CTT CTT AAT AGA CTC GAT 3092 Ar q Ala Gli Ser Ala h I. a. ç'r A Leu Ser Ser Leu Leu Asn Arg Leu Asp 985 990 995 CCC GTG CTT AAA ACT GCA AAT CTA GGA AGT TGG CAG ATT ATC AGT 2140 Pro Vai Leu Arç Lr s Tre Ala Asn Leu Gli Ser Trp Gin Tle Tle Ser .1000 1005 103 0 í'CA. GTT GAA GCC GTT GGA TAT CTT GTe GTT GTG GAT GAG TTG CTT TCA 3130 Pro Vai G J. u Ala Vai G1 i. rir vai Vai. Vai Vai Asp Glu Leu Leu Ser 1015 1020 1025 GTT CAG AAT GAA ATC TAC GAG AAG CCC ACG ATC TTA GTA GCA AAA TCT 3236 Vai Gin Asn Glu Ile Tir Glu Lis Pro Tre Ile Leu Vai Ala Lis Ser 1030 1035 1040 GTT AAA GGA GAG GAG GAA ATT CCT GAT GGT GCT GTT GCC CTG ATA ACA 3284 Vai Lis Gli Glu Glu Glu Ile Pro Asp Gli Ala Vai Ala Leu Ile Tre 1045 1050 1055 1060 CCA GAC ATG CCA GAT prjíjt CTT TCA CAT GTT TCT GTT CGA GCT AGA AAT 3332 Pro Asp Met Pro Asp Vai Leu Ser His Vai Ser Vai Arg AI a Arg Asn 1065 1070 1075 GGG AAG GTT TGC TTT GCT ACA TGC TTT GAT CCC AAT ATA TTG GCT GAC 3380 Gli Lis Vai Cis Fen Ala Tre Cis Fen Asp Pro Asn lie Leu Ala Asp 79 c tc CA A GCA GAG GAA GGA AGG ATT TTG CTC 1 TA AAG CCT ACA CCT TCA 3128 Le j Glu Ais í S Glu Gli Arg Ile Leu Leu L~u Lis Pro Tre Pro Ser 10 9 1100 1105 GAC ATA ATC T.AT ALT GAG GTG AAT GAG ATT GAG CTC CAA AGT TCA AG? 3476 Âsp lie I] 0 T i r ler Gi a vai Asn Gla lie Glu Leu Glu Ser Ser 5 e Γ 11 i i 11V 5 11 2 G. AAC TTG GTA GAA GCT GAA ACT TCA GCA ACA CTT ASA TTG o T G .AAA ΑΛΟ 3524 Asn Leu Vai Glu Ala Glu Tre Ser Ala. Tre Leu Arg Leu Vai Lis Lis 1.12: ::i; 113i ) 1135 1140 CAA TTT GGT GGT TGT TAC GCA ATA TCA GCA GAT GAA TTC ACA AGT GAA T; 0"? Gin Fen GLi Gli Cis Tir Ala Ile Ser Ala Asp Glu Fen Tre Ser Glu 114: 1150 1115 ATG GTT GGA GCT AAA TC A CGT AAT ATT GCA TAT CTG AAA ΑΆΆ GTG 3 620 Met Vai Gli Ala Las Ser Arg Asn lie AI a Tir Leu Lis Gli Lis vai 1160 11 65 ni n CCT TCC TCG GTG GGA ATT CCT /5 A.· Λ7 TCA GTA GCT r' CCA TTT GGA GTC 3 668 Pro Ser Ser Vai Gi i Ile Pro Tre G e r Vai Ala Leu Pro Fen Gli Vai 1175 1 IÃO 1185 TTT GAG AAA GTA CTT TCA GAC GAC ATA AAT CAG GA GTG GCA AAA GA u 7 16 Fen Glu Lis Vai Leu Ser Asp Asp Asp Asn Gin Gli Vai Ala Lis Glu 1190 1195 1200 TTG CAA ATT CTG ATG AAA AAA CTA TCT GAA GGA GAC TTC AGC GCT CTT 3764 Leu Gin Ile Leu Met Lis Lis Leu Ser Glu Gli Asp Fen Ser Ala Leu 1205 1210 1215 1220 GGT GAA ATT CGC ACA ACG GTT TTA GAT CTT TCA GCA CCA GCT CAA TTG 3312 Gli Glu Ile Arg Tre Tre Vai Leu Asp Leu Ser ALLa pro Ala Gin Leu 1225 1230 1235 GTC AAA GAG CTG AAG GAG AAG ATG CAG GGT TCT’ GGC ATG CCT 1 TGG CCT 3860 Vs X Lis Glu Leu Lis Glu Lis Met Gin Gli Ser Gli Met Pro Trp Pro 80 12-:0 1245 1250 CGT GA'·: GAA GGT CCA AAG - A'.-- TGG GAA CAA TGG ATG GCC ATA AAA 3903 Gli Asp GG.u (.-.1. Pro Cis Arg Trp Glu G :T : L.1 Trp Vet: ?- 3 a 1.; e 125. 5 12 6 0 1115 PAG GTG j / : GCT CCA. AAA TGG AAT GAG AGÃ o '...Ρά TAC TTC AGC ACA ACC 3S56 Lis Vai T Χ.Ό lú 3 Ser lis Trp Asn Glu .2 · o 22 a Tir c -·. C e Τ' -- Λ. Arg 12 A - 127: 7.5 128: 1 -Au GTG AAA GTG GAf AAT GAC' TAT CTG J .ο. ATG GCT G W CTT GTT " ΆΑ 4004 Lis Vai Lis Leu Asp His As p Tir Leu C i s Ge c. Ala ’ r .· ! V .'.A . ·.. Lo·-.: Vai Gin 12 6: 5 1290 1 3 9 5 13 0 0 GAA ATA ATA AAT GCT GAT TAT ¢3 CA TTT GTC ATT CAC ΑΓΑ ACC AAC CCA 4052 Glu lie .11 e Asn Ala Asp Tir Ai a Fen V d. ' 11. s His Tre Tre Asn Pro 1 30 5 13 j. 0 131 TCT TCC GGA GAC GAC TCA GAA ATA TAT GCC GAG GTG GTC ÍpacGc GGC CTT 4 100 Ser ser Gli Asp ASp Ser G1 u Ϊ le Tir Ala G i u Vai Vai Arg G.3 ; Leu 1.32 0 1325 1330 GGG GAA ACA CTT GTT GGA GCT TAT CCA GGA CGT GCT TTG AGT TTT ATC 4148 Gli Glu Tre Leu Vai Gli Ala Tir Pro Gli Arg Ala Leu Ser Fen Ile 1335 1340 1345 TGC AAG AAA AAG GAT CTC AAC TCT CCT CAA GTG TTA GGT TAC Ω o > AGC 4196 Cis Lis Lis Lis Asp Leu Asn Ser Pro Gin Vai Leu Gli Tir Pro Ser 1350 1355 1360 AAA CCG ATC GGC CTT TTC ATA AAA AGA TCT ATC ATC TTC CGA TCT GAT 4244 Lis Pro Ile Gli Leu Fen Ile Lis Arg Ser Ile Ile Fen Arg Ser Asp 1365 1370 1375 1380 TCC AAT GGG GAA GAT TTG GAA GGT TAT GCC GGT GCT GGC CTC TAC GAC 4292 Ser Asn Gli Glu Asp Leu Glu Gli Tir Ala Gli Ala Gli Leu Tir Asp 1385 1390 1395 AGT GTA CCA ATG GAT GAG GAG GAA AAA GTT GTA ATT GAT TAC TCT TCC 4340 Ser Vai Pro Met Asp Glu Glu Glu Lis Vai Vai Ile Asp Tir Ser Ser 1400 1405 1410 81 A'.·/1 CCA TTG ATA ACT eAi: GGi AAC τ 7 GGC CAG ACA ATe GTG TCG AAC 4 388 As p Pro lifeu .11 e Tre Asp Gli As:: F e n Arg Glri T r e 1.1 e 1. e u Se: Asn 14": 1 4 2 ( 14 2 3 ATT GCT CGT GOT GGA CA? GCT A'i’;5 GAG GAG GTA ΙΆΤ GGC TíiT CGT CAA 4 4 3 6 Ile Ala A: g Ara G11 His Ala I ie Glu Glu ire:.; Tír Gi.a Ser P ro GG:: L 4 J G 1 λ a 5 1 4 4 G GAC ATA: G?>G 15:?;.' GTA GTG GGG GCT GGA A AG .AT ? 155" GGC: Ge? CAG ACA 4 4 b 4 Asp 11 e G1 u Gi i \'a j. v = j. Avg ASP) Gái Li S Ile Txr Vai "dl Gin Tre 1545 14 5 0 14 5. E 4 CG .ri ri ί i CCA CAG ATG 1 GATTATATT; 5 Ti 5GTTG 45ATG Τ·' TGTTCAGAG AAG 45CCÍA .CAG 4 G 3 7 Arg E-rc G1 n Aer: ATGTGAACAT A Τ T C ΐCAΤT G TAVCAG A?CT GTGACCACTT A- GCTGATACC TC CCATGTiAG 4597 TTACCTGTAT GAG TATilCG T GAT CC AAAGC CATCACATCA TGTTCACOTT CAGCTATIGG 4 65 1 AíGGAGAAGI g AG ΤΑ: G T A G GA A'!11G C Ά A T AT GAGGAArAAT AA.GAAAAACT TTGTAAAAGC 4'717 TAA/iTT.AGCT 15..5.4.1:41 1:5:.1/5 4 AG: 4-:4-5:.5.14/4 TGTGTAAACA TTíiTACTATA TATaG'I5ATAT 4 77? ACACACGCA1' TATGT.AT TGO.A? T ATQCAC1' GAATAATATC GCAGCAlCAA inGAúGAnAl 1. 4B3? CTTTGGGTGG TTTCAAAAA 4 3 56 (2) INFORMAÇÃO PARA A SEQ ID NO: 2: (i) CARACTERÍSTICAS DA SEQUÊNCIA: (A) COMPRIMENTO: 1464 aminoácidos (B) TIPO: Aminoácido (D) TOPOLOGIA: linear (ii) TIPO DE MOLÉCULA: Proteína (xi) DESCRIÇÃO DA SEQUÊNCIA: SEQ ID NO: 2:
Met Ser Asn Ser Leu Glí Asn Asn Leu Leu TIr Gin Glí Fen Leu Tre 1 5 10 15
Ser Tre Vai Leu Glu Hís Lis Ser Arg Ile Ser Pro Pro Cis Vai Gli 20 25 30 82
Gli Asn Ser Leu Ser: Gin 35 Tre Glu Fen Are Gli Asn 50 Meí: G.1 α Lis ·./: s Arg A.:, a 65 Tre Asp Tre Ser Gín Gin. Vsi lie Ser 4 3
Ar q Leu Lr r Vai Gin ler. Ser Seu: Ge.t Pr o 7 5
Air Glu Lis Fen AO
Lis Ser Pro Leu Ser 4 5
Lis Li e Li.e l.Ie Pro 60
His Ala Vai Leu Tre 80
Ser Leu Gli Gli Asn lie Glu Leu Gin Vai Asp Vai Arg Pro Pro Tre Ser Gli Asp Vai Ser 100 105 110
Fen Vai Asp Fen Gin vai Trs Asn Gli Ser Asp Lis Leu Fen. Leu His 115 .120 12:1
Trp Gli Ala Vai. Lis Fen. Gli. Lis Gin Tre Trp Ser Leu Pro Asn Asp 130 35 140
Arg Pro Asp Gli Tre Lis Vai Tir Lis Asn Lis Ala Leu Arg Tre Pro 145 150 155 160
Fen Vai Lis Ser Gli Ser Asn Ser Ile Leu Arg Leu Glu Ile Arg Asp 165 170 175
Tre Ala Ile Glu Ala Ile GluFen Leu lie Tir Asp Glu Ala His Asp 180 185 190
Lis Trp Ile Lis Asn Asn Gli Gli Asn Fen Arg Vai Lis Leu Ser Arg 195 200 205
Lis Glu Ile Arg Gli Pro Asp Vai Ser Vai Pro Glu Glu Leu Vai Gin 210 215 220 ile Gin Ser Tir Leu Arg Trp Glu Arg Lis Gli Lis Gin Asn Tir Pro 225 230 235 240
Glu Tir Glu Ala 250
Pro Glu Lis Glu Lis Glu 245
Ala Arg Tre Vai Leu Gin OCC. Z j -v 83
biU Giu L.LB
Glu Glu Ile A: a Arg Gli Ala Se:’ .1 I o Gin Asp Ile Arg Ala Arg Leu
Tre Lis ?re Am Asp Lis Ser Gin Se,·: Lis LA a GIu Pro Lj:í
Tre Las: 2 ·'- o ·'- ' ο /δ·'1 2 8 5 Ser .Asp Ile Pro Asp Asp Leu Ara Gin Ala Gin Ala Tir Ile 295 300 Arg Trp Gru Lis Ala Gli Lis Pro Asn Tir Pm Pro Glu Lis Gin Ile 30 5 310 LL5 320 Giu Giu Leu Gru Giu Ara Arg Atg Giu Leu Giu Leu Glu Leu Giu Lis 325 33C 335
Gli f ie Ar. ft Leu Asp Glu Leu Aso Lis Tre Lio Tre Lis Gi i Glu Ile 3 4 0 34 5 3 5 r. Lis Tre Lis Vai Glu Lis His Leu Lis Arg Ser Ser Fen Ala Vai Glu 355 360 365 Arg Ile Gin Arg Lis Lis Arg Asp Fen Gli His Leu Ile Asn Lis Tir 370 375 380 Tre Ser Ser Pro Ala Vai Gin Vai Gin Lis Vai Leu Glu Glu Pro Pro 385 390 395 400 Ala Leu Ser Lis Ile Lis Leu Tir Ala Lis Glu Lis Glu Glu Gin Ile 405 410 415 Asp Asp Pro Ile Leu Asn Lis Lis Ile Fen Lis Vai Asp Asp Gli Glu 420 425 430
Leu Leu Vai Leu Vai Ala Lis Ser Ser Gli Lis Tre Lis Vai His Leu 435 440 445
Ala Tre Asp Leu Asn Gin Pro Ile Tre Leu His Trp Ala Leu Ser Lis 450 455 460
Ser Pro Gli Glu Trp Met Vai Pro Pro Ser Ser Ile Leu Pro Pro Gli 465 470 475 480 84
Ser I le 7; e Leu Asp Lis Ala Ala Glu Tre Pro Fen Ser Aia Ser' Ser 1 c 5 490 4 5u Ser Asp. Gli Leu Ire Ser Lis: vai Gin Ser Leu Asp ile 7s 1 lie Glu 5 0 0 505 110
Asp Grl As:; Fen Vai Gli Met Pro t’en Vai Leu Leu ãei Gli. G.iu Las 515 520 555 Gli Se: Asp Fen Tir Vai Gli Fen Ler Ala Ala 535 511' Ser 1.i.s Leu Ala Leu Lis Ala Ala Gli Asp Gli Ser Gli Tre Ala Lis 515 5 50 555 560 Ser Leu Leu Asp Lis Ii.e Ala Asp Met Glu Ser Glu Ala Gin Lis Ser 565 570 575
Fen Met His Arg Fen Asn Ile Ala Ala Asp Leu Ile Glu Asp Ala Tre 580 585 590
Ser Ala Gli Glu Leu Gll Fen Ala Gli Ile Leu Vai Trp Met Arg Fen 595 600 605 Met Ala Tre Arg Gin Leu Ile Trp Asn Lis Asn Tir Asn Vai Lis Pro 610 615 620 Arg Glu Ile Ser Lis Ala G.ln Asp Arg Leu Tre Asp Leu Leu Gin Asn 625 630 635 640 Ala Fen Tre Ser His Pro Gin Tir Arg Glu lie Leu Arg Met Ile Met 645 650 655
Ser Tre Vai Gli Axg Gli Gli Glu Gli Asp Vai Gli Gin Arg Ile Arg 660 665 670 Asp Glu Ile Leu Vai Ile Gin Arg Asn Asn Asp Cis Lis Gli Gli Met 675 680 685
Met Gin Glu Trp His Gin Lis Leu His Asn Asn Tre Ser Pro Asp Asp 690 695 700 85
Vai Vai Ile Cies Gin A'·-a Leu 7 1 705 710
Leu Gli Vai Tir Tcp Lis ?re Lgu 72 5 A.rg Iieu Leu Ger Tir Asp Arg Ala 7 4 0
Gli Asp Gin Lis Gli Gli Leu Leu 755 750
Tre Leu Lis Ala vai His Ser Gli 770 775
Asn Cis Met G-li Tir Lis Tre Giu 785 790
Gin Ile Asn Pro Vai Ser Gli Leu 805
His Fen Vai Leu Asp His Vai Glu 820
Glu Arg Leu Leu Glu Ala Ala Glu 835 840
Pro Asn Asn Arg Leu Lis Asp Leu 850 855
Ser Tre Vai Arg Tre Ala Vai Glu 865 870
Ala Asn Pro Glu Lis Ile Met Tir 885
Leu Ala Leu Ser Vai Asp Asp Asn 900
Gli Trp Asn Gin Ala Leu Ser Met 2 Asp 'rir Ile Lia Ger Asp Fen Asp 715 720
Asn Glu Asn G7: ile Tre 2is Glu 730 725
Ile His Ser Giu Pro Asn Fen Arg 745 750
Arg Asp Leu Gli Mis Tir Met Arg
-? " C v : -j
Ala Asp Leu Giu Ger Ala Ile Ala 7 30
Gli Glu Gli Fen Met Vai Gli Vai 795 800
Pro Ser Gli Fen Gin Asp Leu Leu 810 815
Asp Lis Asn Vai Glu Tre Leu Leu 825 830
Glu Leu Arg Pro Leu Leu Leu Lis 845
Leu Fen Leu Asp lie Ala Leu Asp 860
Arg Gli Tir Glu Glu Leu Asn Asn 875 880
Fen Ile Ser Leu Vai Leu Glu Asn 890 895
Glu Asp Leu Vai Tir Cis Leu Lis 905 910
Ser Asn Gli Gli Asp Asn His Trp 86 92 5
η 5 92 G
Ala Leu Fer; AJ..a Las AI a V'al Leu Asp Arg lave Arg Leu Ala .Leu .Ala 930 935 940
Sea Lis Ala G1u Tio Tir Kis His Leu Leu Gin Pro Ser Ala Glu Tir 945 950 955 960
Leu Glí Ser Ile Leu Gli Vai Asp Gin Trp Ai a Leu Asn Ile len Tre 965 97C 995
Glu Glu Ile Ile Arg Ala Gli Ser Ala AI; Leu Ser Ser Leu Leu 980 085 990
Asn Arg Leu Asp Pro Vai Leu Arg Lis Tre Ala Asn Leu Gli Ser Trp 995 1000 1005
Gin Ile Ile 1010 Ser Pro Vai Glu Ala 1015 Vai Gli Tir Vai Vai 1020 Vai Vai Asp Glu Leu Leu Ser Vai Gin Asn Glu Ile Tir Glu Lis Pro Tre Ile Leu 1025 1030 1035 1 .040
Vai Ala Lis Ser Vai Lis Gli Glu Glu Glu Ile Pro Asp Gli Ala Vai 1045 1050 1055
Ala Leu Ile Tre Pro Asp Met Pro Asp Vai Leu Ser His Vai Ser Vai 1060 1065 1070
Arg Ala Arg Asn Gli Lis Vai Cis Fen Ala Tre Cis Fen Asp Pro Asn 1075 1080 1085
Ile Leu Ala Asp Leu Gin Ala Lis Glu Gli Arg Ile Leu Leu Leu Lis 1090 1095 1100
Pro Tre Pro Ser Asp Ile Ile Tir Ser Glu Vai Asn Glu Ile Glu Leu 1105 1110 1115 1120
Gin Ser Ser Ser Asn Leu Vai Glu Ala Glu Tre ser Ala Tre Leu Arg 1125 1130 1135 87
Leu
Li s
Lis Gin t'en Gii Gli Cis Tír AI a I];? Ler Ala Asp Gi.u i 14 0 1145 1150 Fen ire Ser Glu Met vai Gli Ala Lis Ser Arg Asn Ile Ala Tir Leu i 155 1160 1165 Lis Gii Lis vai Pro Sei Ser Vai Gii Ile Pro T/e Ser Vai Ala Leu i IV ϋ O GO Pro Fen Gli Ya L Fen Glu los Vai Los; Lar A.sp uso lie Asn Gin Gii 113 5 1190 1195 i 200 Va.i Ala Lis GJu Leu Gli; lie Leu Met Lis Lis leu Ser Glu Gii Pisp 1. 2 0 1210 1215
Fer Ser Ala Leu 31 :i. Glu Ile Arg Tre Tre Vai Leu Asp Leu Ser Ala 1220 1225 1230 Pro Ala Gin Leu Vai Lis Glu Leu Lis Glu Lis Met Gin Gli Ser Gli 1235 1240 1245
Met Pro Trp Pro Gli Asp Glu Gli Pro Lis Arg Trp Glu Gin Ala Trp 1250 1255 1260 Met Ala Ile Lis Lis Vai Trp Ala Ser Lis Trp Asn Glu Arg Ala Tir 1265 1270 1275 1290 Fen Ser Tre Arg Lis Vai Lis Leu Asp His Asp Tir Leu Cis Met Ala 1285 1290 1295
Vai Leu Vai Gin Glu Ile Ile Asn Ala Asp Tir Ala Fen Vai Ile His 1300 1305 1310 Tre Tre Asn Pro Ser Ser Gli Asp Asp Ser Glu Ile Tir Ala Glu Vai 1315 1320 1325
Vai Arg Gli Leu Gli Glu Tre Leu Vai Gli Ala Tir Pro Gli Arg Ala 1330 1335 1340
Leu Ser Fen Ile Cis Lis Lis Lis Asp Leu Asn Ser Pro Gin Vai Leu 1345 1350 1355 1360
Fr o Ser
Je G.l r Leu Fen lie Lis Arg Ler Lie 1. 137 0 í. 37 5
Ftn Arg Ler Asp Ser As:
Glu Asp I38i
UrU LAI li.
Lr i Leu Air Asp Ler Lai. Pro Met Ast> Llu Glu Glu Lrs Ver. vai L...e IreLu ;. 4 i r ΰ .5.4 OS
Asp LAr Ser Ler Ρερ Pro Leu Ile Tre Asp GL 8 Asa ter: Arq LAn. Ire ] 4 10 1413 1. 4 2 C lie Leu Ser Asn Ire Ala Arq Sia G.li. IPis Ala Ile Glu Glu Leu Tír 1425 1430 1435 3340
Gli Ser Pro Gin Asp Ile Glu Gli Vai Vai Arg Asp Gli Lis Ile Tir 1445 1450 1455
Vai Vai Gin Tre Arg Pro Gin Met 1460 (2) INFORMAÇÃO PARA A SEQ ID NO: 3: (i) CARACTERÍSTICAS DA SEQUÊNCIA: (A) COMPRIMENTO: 1918 pares de bases (B) TIPO: nucleótido (C) ESTRUTURA HELICOIDAL: estrutura helicoidal simples (D) TOPOLOGIA: linear (ii) TIPO DE MOLÉCULA: ADNc a ARNm (vi) FONTE ORIGINAL: (A) ORGANISMO: Solanum tuberosum (B) ESTIRPE: C.V. Desiree (íx) CARACTERÍSTICA:
(A) NOME/CHAVE: CDS 89 : B ) LOCALIZAÇÃO: 1, (xi / DESCRI ÇÃO DA 5EQUÈNC ^ ]'A: SEQ ID NC ): 3 GCA GAG TGG TAC GAT CAC T?A TTG CAG OCA TCT GCC TAT -•r- y GFA 4 8 Ala j Giu Trp T.i r G.i Hir Leu Leu Gin ÍC y Ser Gin V :.\i T i r o r.; Gli TCA ATA CTT GTG GAC CAA TGG GCT Vi AAC ATA TTT ACT CAA GÕA 96 Ser Ile Leu Vai Asp Gin Trp Ala Oc; u Asn Ile Fen Tre G.i u Gi u 10 25 30 ATT ATA CGT GCT GGA TCA GCA GCT TCA TTA TCC TCT CTT CTT AAT AGA 144 Ile Ile Arg Ala Gli Ser Ala Ala Ser Leu Ser Ser Leu Leu Asn Arg 35 40 45 CTC GAT CCC GTG CTT CGG AAA ACT GCA AAT CTA GGA AGT TGA CAG ATT 192 Leu Asp Pro Vai Leu Arg Lis Tre Ala Asn Leu Gli Ser Trp Gin Ile 50 55 60 ATC AGT CCA GTT GAA GCC GTT GGA TAT GTT GTC GTT GTG GAT GAG TTG 240 Ile Ser Pro Vai Glu Ala Vai Gli Tir Vai Vai Vai Vai Asp Glu Leu 65 70 75 80 CTT TCA GTT CAG AAT GAA ATC TAC GAG AAG CCC ACG ATC TTA GTA GCA 288 Leu Ser Vai Gin Asn Glu Ile Tir Glu Lis Pro Tre Ile Leu Vai AI CL 85 90 95 AAA TCT GTT AAA GGA GAG GAG GAA ATT CCT GAT GGT GCT GTT GCC CTG 336 Lis Ser Vai Lis Gli Glu Glu Glu Ile Pro Asp Gli Ala Vai Ala Leu 100 105 110 ATA ACA GCA GAG ATG CCA GAT GTT CTT TCA CAT GTT TCT GTT CG A GCT 384 Ile Tre Pro Asp Met Pro Asp Vai Leu Ser His Vai Ser Vai Arg AI a 115 120 125 AGA AAT GGG AAG GTT TGC TTT GCT ACA TGC TTT GAT CCC AAT ATA rp ç* r"p 432 Arg Asn Gli Lis Vai Cis Pen Ala Tre Cís Fen Asp Pro Asn Ile Leu 130 135 140 90 GCT GAC CTC CAI'. GCA AAG GAA GGA aGG ATT TTG ccc TTA PAG CCT ACA 4 80 Ala Asp Leu Gin Ale L i. s Glu Gli Arg Ile Leu Lr a Leu Li s 1 ro Tre 1 4 L 150 155 160 CCT TCA GAC ATA ATC TAT AGT GAG GTG AAT ee l:. ~T'T GAG CTC CL A. AGT 3 u. Pr o O ÍG 1. Asp lie 11 e Tir Ser G 1 u Vai Asn Glu 7 le Cru Leu Cn Ser 165 170 - "7 c TCA LGT AAC TTG GTA GAA GCT GAA AGT TCA : ; „ ACA CTT AGA TTG GTG 5 7 6 T e :r Ser Asn Leu Vai Glu AC 3 Glu Tre Ser Ala T re Leu Arg Le a Vai 10 0 185 j. 80 AAA AAG CAA TTT GGT GGT TGT TAC GCA ATA TCA GCA GAT GAA TTC ACA 624 Lis Lis Gin Fen Gli Gli Cis Tir AI a Ile Ser Ala Asp Glu Fen Tre 195 200 205 AGT GAA ATG GTT GGA GCT AAA TCA CGT AAT ATT GCA TAT CTG AAA GGA 672 Ser Glu Met Vai Gli Ala Lis Ser Arg Asn Ile AI a Tir Leu Lis Gli 210 215 220 AAA GTG CCT TCC TCG GTG GGA ATT CCT ACG TCA GTA GCT CTT CCA TTT 720 Lis Vai pro Ser Ser Vai Gli Ile Pro Tre Ser Val AI a Leu Pro Fen 225 230 235 240 GGA GTC TTT GAG AAA GTA CTT TCA GAC GAC ATA AAT CAG GGA GTG GCA 768 Gli Vai Fen Glu Lis Vai Leu Ser Asp Asp Ile Asn Gin Gli Val Ala 2 4 5 250 255 AAA GAG TTG CAA ATT CTG ACA AAA AAA CTA TCT GAA GGA GAC TTT AGC 816 Lis Glu Leu Gin X le Leu Tre Lis Lis Leu Ser Glu Gli Asp Fen Ser 260 265 270 GCT CTT GGT GAA ATT GGC ACA ACG GTT TTA GAT CTT TCG ACA CCA GCT 864 Ala Leu Gli Glu X le Arg Tre Tre Val Leu Asp Leu Ser Tre Pro Ala 275 280 285 CAA TTG GTC AAA GAG CTG AAG GAG AAe ATG CAG GGT TCT GGC ATG CCT 912 Gin Leu Vai Lis Glu Leu Lis Glu Lis Met Gin Gli Ser Gli Met Pro 290 295 300 TGG CCT GGTGAT GAA GGT CCA AAG CGG TGG GAA CAA GCA TGG ATG GCC 960 91
Trp Pro Gli Asp Glu Gli Pro Lis Arg Trp Glu Gin AI a Trp Met Ala 305 310 315 320 ΑΤΑ AAA AAG GTG TGG GCT TCA AAA TGG AAT GAG AGA GCA TAC TTC AGC 1008 Ile Lis Lis Vai Trp Ala Ser Lis Trp Asn Glu Arg Ala Tir Fen Ser 325 330 335 ACA AGG AAG GTG AAA CTG GAT CAT GAC TAT CTG TGC ATG GCT GTC CTT 1056 Tre Arg Lis Vai Lis Leu Asp His Asp Tir Leu Cis Met Ala Val Leu 340 345 350 GTT CAA GAA ATA ATA AAT GCT GAT TAT GCA TTT GTC ATT CAC ACA ACC 1104 Vai Gin Glu Ile Ile Asn Ala Asp Tir Ala Fen Vai Ile His Tre Tre 355 360 355 AAC CCA TCT TCC GGA GAC GAC TCA GAA ATA TAT GCC GAG GTG GTC AGG 1152 Asn Pro Ser Ser Gli Asp Asp Ser Glu Ile Tir Ala Glu Val Val Arg 370 375 380 GGC CTT GGG GAA ACA CTT GTT GGA GCT TAT CCA GGA CGT CGT TTG AGT 1200 Gli Leu Gli Glu Tre Leu Vai Gli Ala Tir Pro Gli Arg Ala Leu Ser 385 390 395 400 TTT ATC TGC AAG AAA AAG GAT CTC AAC TCT CCT CAA GTG TTA GGT TAC 1248 Fen Ile Cis Lis Lis Lis Asp Leu Asn Ser Pro Gin Val Leu Gli Tir 405 410 415 o o > AGC AAA CCG ATC GGC CTT TTC ATA AAA AGA TCT ATC ATC TTC CGA 1296 Pro Ser Lis Pro Ile Gli Leu Fen Ile Lis Arg Ser Ile Ile Fen Arg 420 425 430 TCT GAT TCC AAT GGG GAA n t\ m u/ii TTG GAA GGT TAT GCC GGT GCT GGC CTC 1344 Ser Asp Ser Asn Gli Glu Asp Leu Glu Gli Tir Ala Gli Ala Gli Leu 435 440 445 TAC GAC AGT GTA CCA ATG aAT GAG GAG GAA AAA GTT GTA ATT GAT TAC 1392 Ti r Asp Ser Vai Pro Met Asp Glu Glu Glu Lis Vai Val Ile Asp Tir 450 455 460 TCT TCC GAC CCA Ttg ATA ACT GAT GGT AAC TTC CGC CAG ACA ATC CTG 1440 Ser Ser Asp Pro Leu Ile Tre Asp Gli Asn Fen Arg Gln Tre Ile Leu 92 465 470 475 480 O O AAC ATT GCT CG A GCT GGA CAT GCT ATC GAG GAG CTA TAT GGC TCT 1488 Ser Asa Ile Ala Arg Ala Gli His Ar a Ile Glu Glu Leu Tir Gli Ser 485 490 495 o o >-3 CAA GAC ATT GAG GGT GTA GTG AGG GAT GGA AAG ATT TAT GTC GTT 1536 Pro Gin Asp Ile Glu Gli Vai Vai Arg Asp Gli Lis rle Tir Vai Vai 500 505 510 CAG ACA AGA CCA CAG ATG T GATTATATTC TCGTrGTATG TTGTTCAGAG 1585 Gin Tre Arg Pro Gin Met 515 AAGACCACAG ATGTGATCAT ATTCTCATTG TATCAGATCT GTGACCACTT ACCTGATACC 1645 TCCCATGAAG TTACCTGTAT GATTATACGT GATCCAAAGC CATCACATCA TGTTCACCTT 1705 CAGCTATTGG AGGAGAAGTG AGAAGTAGGA ATTGCAATAT GAGGAATAAT AAGAAAAACT 1765 TTGTAAAAGC TAAATTAGCT GGGTATGATA TAGGGAGAAA TGTGTAAACA TTGTACTATA 1825 TATAGTATAT ACACACGCAT TATGTATTGC ATTATGCACT GAATAATATC GCAGCATCAA 1885 AGAAGAAATC CTTTGGGTGG TTTCAAAAAA AAA 1918 (2) INFORMAÇÃO PARA A SEQ ID NO: 4: (i) CARACTERÍSTICAS DA SEQUÊNCIA: (A) COMPRIMENTO: 518 aminoácidos (B) TIPO: aminoácido (D) TOPOLOGIA: linear (ii) TIPO DE MOLÉCULA: proteína (xi) DESCRIÇÃO DA SEQUÊNCIA: SEQ ID NO: 4:
Ala Glu Irp Tir His His Leu Leu Gin Pro ser Ala Glu Tir Leu Gli 15 10 15 93
Ser Ile Leu Gli Vai Asp Gin Trp Ala Leu Asn Ile Fen Tre Glu Glu 20 25 30
Ile Ile Arg Ala Gli Ser Ala Ala Ser Leu Ser Ser Leu Leu Asn Arg 35 40 45
Leu Asp Pro Vai Leu Arg Lis Tre Ala Asn Leu Gli Ser Trp Gin Ile 50 55 60
Ile Ser Pro Vai Glu Ala Vai Gli Tir Vai Vai Vai Vai Asp Glu Leu 65 70 75 80
Leu Ser Vai Gin Asn Glu Ile Tir Glu Lis Pro Tre Ile Leu Vai Ala 85 90 95
Lis Ser Vai Lis Gli Glu Glu Glu Ile Pro Asp Gli Ala Vai Ala Leu 100 105 110
Ile Tre Pro Asp Met Pro Asp Vai Leu Ser His Vai Ser Vai Arg Ala 115 120 125
Arg Asn Gli Lis Vai 130
Ala Asp Leu Gin Ala 145
Pro Ser Asp Ile Ile 165
Cis len Ala Tre Cis 135
Lis Glu Gli Arg Ile 150
Tir Ser Glu Vai Asn 170
Fen Asp Pro Asn Ile Leu 140 Leu Leu Leu Lis Pro Tre 155 160 Glu Ile Glu Leu Gin Ser 175
Ser Ser Asn Leu Vai Glu Ala Glu 180
Lis Lis Gin Fen Gli Gli Cis Tir 195 200
Ser Glu Met Vai Gli Ala Lis Ser 210 215
Lis Vai Pro Ser Ser Vai Gli Ile 225 230
Tre Ser Ala Tre Leu Arg Leu Vai 185 190
Ala Ile Ser Ala Asp Glu Fen Tre 205
Arg Asn Ile Ala Tir Leu Lis Gli 220
Prc· Tre Ser Vai Ala Leu Pro Fen 235 240 94
Gli Vai Fen Glu Lis Vai Leu Ser Asp Asp Ile Asn Gin Gli Vai Ala 245 250 255
Lis Glu Leu Gin Ile Leu Tre Lis Lis Leu Ser Glu Gli Asp Fen Ser
Ala Leu Gli 260 265 270 Glu Ile Arg Tre Tre Vai Leu Asp Leu Ser Tre Pro Ala 275 280 285
Gin Leu Vai Lis Glu Leu Lis Glu Lis Met Gin Gli Ser Gli Met Pro 290 295 300 Trp Pro Gli Asp Glu Gli Pro Lis Arg Trp Glu Gin Ala Trp Met Ala 305 310 315 320 Ile Lis Lis Vai Trp Ala Ser Lis Trp Asn Glu Arg Ala Tir Fen Ser 325 330 335 Tre Arg Lis Vai Lis Leu Asp His Asp Tir Leu Cis Met Ala Vai Leu 340 345 350
Vai Gin Glu Ile Ile Asn Ala Asp Tir Ala Fen Vai Ile His Tre Tre 355 360 365 Asn Pro Ser Ser Gli Asp Asp Ser Glu Ile Tir Ala Glu Vai Vai Arg 370 375 380 Gli Leu Gli Glu Tre Leu Vai Gli Ala Tir Pro Gli Arg Ala Leu Ser 385 390 395 400
Fen Ile Cis Lis Lis Lis Asp Leu Asn Ser Pro Gin Vai Leu Gli Tir
Pro Ser Lis 405 410 415 Pro Ile Gli Leu Fen Ile Lis Arg Ser Ile Ile Fen Arg 420 425 430
Ser Asp Ser Asn Gli Glu Asp Leu Glu Gli Tir Ala Gli Ala Gli Leu 435 440 445
Tir Asp Ser Vai Pro Met Asp Glu Glu Glu Lis Vai Vai Ile Asp Tir 450 455 460 95
Ser Ser Asp Pro Leu Ile Tre Asp Gli Asn Fen Arg Gin Tre Ile 465 470 475
Ser Asn Ile Ala Arg Ala Gli His Ala Ile Glu Glu Leu Tir Gli 485 490 495 ..is Ile Tir Vai
Leu 480 Ser Vai
Pro Gin Asp Ile Glu Gli Vai Vai Arg Asp 500 505
Gin Tre Arg Pro Gin Met 515
Lisboa, 14 de Setembro de 2006 96
Claims (27)
- REIVINDICAÇÕES 1. Molécula de ácido nucleico que codifica uma proteína que está presente em células de plantas sob uma forma ligada a grânulos de amido, assim como sob uma forma solúvel e cuja redução, nas células das plantas, conduz à síntese de um amido que exibe um teor de fosfato reduzido ou que leva à expressão na E. coli até à fosforilação do glicogénio sintetizado dentro das células, caracterizada pelo facto de se seleccionar em: (a) moléculas de ácidos nucleicos que codificam uma proteína com a sequência de aminoácidos indicada na SEQ ID N° 2; (b) moléculas de ácidos nucleicos que compreendem a região de codificação da sequência de nucleótidos indicada na SEQ ID N° 1; (c) moléculas de ácidos nucleicos que hibridizam com as moléculas de ácido nucleico mencionadas em (a) e (b) (d) moléculas de ácidos nucleicos de (C), em que a hibdridização tem lugar em condições severas. (e) moléculas de ácidos nucleicos cuja sequência é pelo menos 60 % idêntica à da região de codificação da sequência de nucleótidos indicada na SEQ ID N° 1; e (f) fragmentos das moléculas de ácidos nucleicos mencionadas em (a) a (d), em que os referidos fragmentos têm um comprimento suficiente para codificar uma proteína que está presente em células de plantas sob a forma ligada a grânulos de amido, 1 assim como sob a forma solúvel e cuja redução nas células das plantas leva à síntese de um amido que exibe um teor de fosfato reduzido ou que conduz, após expressão em E. coli, à fosforílação de glicogénio sintetizado dentro das células.
- 2. Molécula de ácido nucleico, de acordo com a reivindicação 1 (e) , caracterizada pelo facto de a identidade da sequência ser de pelo menos 80 %.
- 3. Molécula de ácido nucleico, de acordo com a reivindicação 2, caracterizada pelo facto de a identidade da sequência ser maior do que 90 %.
- 4. Vector caracterizado pelo facto de conter uma molécula de ácido nucleico de acordo com uma qualquer das reivindicações 1 a 3.
- 5. Vector, de acordo com a reivindicação 4, caracterizado pelo facto de a molécula de ácido nucleico estar ligada a elementos reguladores que asseguram a transcrição em células eucarióticas ou procarióticas.
- 6. Célula hospedeira caracterizada pelo facto de estar geneticamente modificada com uma molécula de ácido nucleico de acordo com uma qualquer das reivindicações 1 a 3 ou com um vector de acordo com as reivindicações 4 ou 5.
- 7. Célula de planta transgénica, caracterizada pelo facto de estar transformada com uma molécula de ácido nucleico de acordo com uma qualquer das reivindicações 1 a 3, que está ligada aos elementos de ADN reguladores que asseguram a transcrição em células de plantas. 2
- 8. Planta transgéníca caracterizada pelo facto de compreender células de plantas transgénicas de acordo com a reivindicação 7.
- 9. Material de propagação de plantas, de acordo com a reivindicação 8, caracterizado pelo facto de compreender células de plantas de acordo com a reivindicação 7.
- 10. Processo de produção de uma proteína caracterizada pelo facto de estar presente nas células de plantas sob a forma ligada a grânulos de amido, em que a célula hospedeira, de acordo com a reivindicação 6, é cultivada em condições que permitem a expressão da proteína e em que a proteína é isolada das células e/ou do meio de cultura.
- 11. Proteína caracterizada pelo facto de ser codificada por uma molécula de ácido nucleico de acordo com uma qualquer das reivindicações 1 a 3 ou que se pode obter pela expressão de uma molécula de ácido nucleico de acordo com uma qualquer das reivindicações 1 a 3 num processo de acordo com a reivindicação 10.
- 12. Anticorpo caracterizado pelo facto de reconhecer especificamente a proteína de acordo com a reivindicação 11.
- 13. Molécula de ADN caracterizada pelo facto de codificar (a) um ARN de sentido inverso complementar aos transcritos de uma molécula de ADN de acordo com uma qualquer das reivindicações 1 a 3; ou 3 (b) um ARN que exibe uma actividade de ribozima que cliva especificamente os transcritos de uma molécula de ADN de acordo com uma qualquer das reivindicações 1 a 3; ou (c) uma molécula de ARN que, após expressão numa célula de plantas conduz a uma redução da expressão de uma molécula de ácido nucleico de acordo com uma qualquer das reivindicações 1 a 3, devido ao efeito de co-supressâo e que exibe um elevado grau de homologia com os transcritos da referida molécula de ácido nucleico, na condição de que a molécula de ADN não é a molécula ggctcaggggggttattctg ctttacctag (os últimos 30 nucleótidos dos oito intrões do gene Hnf-1 de rato) ou a molécula gccttgtgggaacacttgttagagttgggcaaa (região V re-arranjada da cadeia humana de TCR-gama).
- 14. Vector caracterizado pelo facto de compreender uma molécula de ADN de acordo com a reivindicação 13.
- 15. Vector, de acordo com a reivindicação 14, caracterizado pelo facto de a molécula de ADN estar combinada com elementos reguladores de ADN que asseguram a transcrição em células de plantas.
- 16. Célula hospedeira, caracterizada pelo facto de compreender uma molécula de ADN de acordo com a reívindicção 13 ou um vector, de acordo com a reivindicação 14 ou 15. 4
- 17. Célula de planta transgénica caracterizada pelo facto de compreender: (a) uma molécula de ADN que codifica um ARN de sentido inverso que é complementar aos transcritos de uma molécula de ADN de acordo com uma qualquer das reivindicações 1 a 3 e que inibe a expressão de uma molécula de ácido nucleico de acordo com uma qualquer das reivindicações 1 a 3, na célula; ou (b) uma molécula de ADN que codifica um ARN que exibe uma actividade de ribozima que cliva especificamente os transcritos de uma molécula de ácido nucleico de acordo com uma qualquer das reivindicações 1 a 3; ou (c) uma molécula de ADN que codifica um ARN que, após a expressão numa célula de planta, conduz à redução da expressão de uma molécula de ácido nucleico de acordo com uma qualquer das reivindicações 1 a 3, devido ao efeito de co-supressão e que exibe um elevado grau de homologia com os transcritos da referida molécula de ácido nucleico. em combinação com elementos reguladores de ADN que asseguram a transcrição em células de plantas.
- 18. Planta transgénica caracterizada pelo facto de se poder obter por regeneração de uma célula de planta de acordo com a reivindicação 17 e contendo células de plantas de acordo com a reivindicação 17. 5
- 19. Molécula de ARN caracterizada pelo facto de se poder obter por transcrição de uma molécula de ADN de acordo com a reivindicação 13.
- 20. Material de propagação de plantas, de acordo com a reivindicação 18, caracterizado pelo facto de conter células de plantas de acordo com a reivindicação 17.
- 21. Planta transgénica de acordo com a reivindicação 18, caracterizada pelo facto de ser uma planta de batata.
- 22. Tubérculo de uma planta de batata caracterizado pelo facto de estar de acordo com a reivindicação 21.
- 23. Tubérculo de acordo com a reivindicação 22, caracterizado pelo facto de, em comparação com os tubérculos das plantas de tipo selvagem, exibir um adoçamento a frio reduzido.
- 24. Utilização de um tubérculo de batata de acordo com as reivindicações 22 ou 23, caracterizada pelo facto de se destinar à produção de batatas fritas em palitos ou em rodelas.
- 25. Utilização de uma molécula de ADN que codifica um ARN de sentido inverso que é complementar aos transcritos de uma molécula de ADN de acordo com uma qualquer das reivindicações 1 a 3, caracterizada pelo facto de se destinar à produção de uma planta transgénica de acordo com a reivindicação 18.
- 26. Utilização de uma molécula de ADN que codifica um ARN com actividade de ribozíma que cliva especificamente os transcritos de uma molécula de ADN de acordo com uma 6 qualquer das reivindicações 1 a 3 caracterizada pelo facto de se destinar à produção de uma planta transgénica de acordo com a reivindicação 18.
- 27. Utilização de uma molécula de ADN que codifica um ARN que, após a expressão numa célula de planta, conduz à redução da expressão de uma molécula de ácido nucleico de acordo com uma qualquer das reivindicações 1 a 3, devida ao efeito de co-supressão e que exibe um elevado grau de homologia com os transcritos da referida molécula de ácido nucleico, caracterizada pelo facto de se destinar à produção de uma planta transgénica de acordo com a reivindicação 18. Lisboa, 14 de Setembro de 2006
Applications Claiming Priority (2)
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| DE19534759A DE19534759A1 (de) | 1995-09-19 | 1995-09-19 | Pflanzen, die eine modifizierte Stärke synthetisieren, sowie Verfahren zu ihrer Herstellung |
| DE19547733A DE19547733A1 (de) | 1995-12-20 | 1995-12-20 | Pflanzen, die eine modifizierte Stärke synthetisieren, Verfahren zu ihrer Herstellung sowie modifizierte Stärke |
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| PT04002725T PT1435205E (pt) | 1995-09-19 | 1996-09-19 | Plantas que sintetizam um amido modificado, processo para a sua produção e amido modificado |
| PT96932575T PT851934E (pt) | 1995-09-19 | 1996-09-19 | Plantas que sintetizam um amido modificado, processo para a sua produção e amido modificado |
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1996
- 1996-09-19 DE DE59611501T patent/DE59611501D1/de not_active Expired - Lifetime
- 1996-09-19 AU AU71313/96A patent/AU715944B2/en not_active Expired
- 1996-09-19 DK DK96932575T patent/DK0851934T3/da active
- 1996-09-19 DK DK04002725.2T patent/DK1435205T3/da active
- 1996-09-19 EP EP04002725A patent/EP1435205B1/de not_active Expired - Lifetime
- 1996-09-19 ES ES96932575T patent/ES2264143T3/es not_active Expired - Lifetime
- 1996-09-19 EP EP06013739A patent/EP1728441A3/de not_active Withdrawn
- 1996-09-19 JP JP51147997A patent/JP4118330B2/ja not_active Expired - Lifetime
- 1996-09-19 WO PCT/EP1996/004109 patent/WO1997011188A1/de not_active Ceased
- 1996-09-19 AT AT96932575T patent/ATE332382T1/de active
- 1996-09-19 HU HU9900510A patent/HU229777B1/hu unknown
- 1996-09-19 EP EP96932575A patent/EP0851934B1/de not_active Expired - Lifetime
- 1996-09-19 EP EP05024607A patent/EP1702518A1/de not_active Withdrawn
- 1996-09-19 PT PT04002725T patent/PT1435205E/pt unknown
- 1996-09-19 PT PT96932575T patent/PT851934E/pt unknown
- 1996-09-19 CA CA2231774A patent/CA2231774C/en not_active Expired - Lifetime
- 1996-09-19 AT AT04002725T patent/ATE447855T1/de active
- 1996-09-19 ES ES04002725T patent/ES2335494T3/es not_active Expired - Lifetime
- 1996-09-19 DE DE59611362T patent/DE59611362D1/de not_active Expired - Lifetime
-
1998
- 1998-03-19 US US09/045,360 patent/US6207880B1/en not_active Expired - Lifetime
-
2000
- 2000-12-21 US US09/746,390 patent/US6815581B2/en not_active Expired - Lifetime
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2003
- 2003-12-30 US US10/750,161 patent/US7176190B2/en not_active Expired - Fee Related
-
2005
- 2005-11-18 US US11/281,861 patent/US20060168691A1/en not_active Abandoned
-
2006
- 2006-10-19 US US11/583,077 patent/US7897760B2/en not_active Expired - Fee Related
- 2006-10-20 US US11/583,839 patent/US7569744B2/en not_active Expired - Fee Related
-
2008
- 2008-02-08 JP JP2008028262A patent/JP2008173128A/ja active Pending
- 2008-11-14 US US12/271,255 patent/US20100174061A1/en not_active Abandoned
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2010
- 2010-12-28 US US12/979,894 patent/US8586722B2/en not_active Expired - Fee Related
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