DK172400B1 - Fremgangsmåde til fremstilling af renset minactivin, minactivinkodende DNA-molekyle, rekombinant DNA-molekyle, sammensmeltet gen, vært, reagent til lokalisering og definering af grænserne for tumorer i histologiske prøver, samt anvendelse af det rekombinante DNA-molekyle, minactivinet og peptider deraf - Google Patents

Fremgangsmåde til fremstilling af renset minactivin, minactivinkodende DNA-molekyle, rekombinant DNA-molekyle, sammensmeltet gen, vært, reagent til lokalisering og definering af grænserne for tumorer i histologiske prøver, samt anvendelse af det rekombinante DNA-molekyle, minactivinet og peptider deraf Download PDF

Info

Publication number: DK172400B1
Authority: DK; Denmark
Prior art keywords: minactivin; ser; leu; glu; ala
Prior art date: 1986-03-13

Application number

DK595187A

Other languages

Danish (da)

English (en)

Other versions

DK595187A (da

DK595187D0 (da

Inventor

Toni Marie Antalis

Thomas Michael Barnes

Michelle Alison Clark

Peter Leonard Devine

Neil Howard Goss

Philip Ralph Lehrbach

Original Assignee

Biotech Australia Pty Ltd

Univ Australian

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1986-03-13

Filing date

1987-11-13

Publication date

1998-05-18

1987-11-13 Application filed by Biotech Australia Pty Ltd, Univ Australian filed Critical Biotech Australia Pty Ltd

1987-11-13 Publication of DK595187D0 publication Critical patent/DK595187D0/da

1988-07-21 Publication of DK595187A publication Critical patent/DK595187A/da

1998-05-18 Application granted granted Critical

1998-05-18 Publication of DK172400B1 publication Critical patent/DK172400B1/da

Links

108010087673 minactivin Proteins 0.000 title claims abstract description 263
108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 38
102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 28
108020004511 Recombinant DNA Proteins 0.000 title claims abstract description 20
238000004519 manufacturing process Methods 0.000 title claims abstract description 15
108020004414 DNA Proteins 0.000 title claims description 33
206010028980 Neoplasm Diseases 0.000 title claims description 23
102000053602 DNA Human genes 0.000 title claims description 21
239000003153 chemical reaction reagent Substances 0.000 title claims description 11
108700026220 vif Genes Proteins 0.000 title description 2
108090000623 proteins and genes Proteins 0.000 claims abstract description 81
230000014509 gene expression Effects 0.000 claims abstract description 31
108091028043 Nucleic acid sequence Proteins 0.000 claims description 78
210000004027 cell Anatomy 0.000 claims description 69
102000004169 proteins and genes Human genes 0.000 claims description 60
238000000034 method Methods 0.000 claims description 57
230000000694 effects Effects 0.000 claims description 55
102000003990 Urokinase-type plasminogen activator Human genes 0.000 claims description 51
108090000435 Urokinase-type plasminogen activator Proteins 0.000 claims description 51
229960005356 urokinase Drugs 0.000 claims description 51
DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 43
239000012634 fragment Substances 0.000 claims description 30
239000013612 plasmid Substances 0.000 claims description 30
150000001413 amino acids Chemical group 0.000 claims description 29
239000000047 product Substances 0.000 claims description 29
238000010828 elution Methods 0.000 claims description 26
239000006228 supernatant Substances 0.000 claims description 26
238000013519 translation Methods 0.000 claims description 25
230000004071 biological effect Effects 0.000 claims description 21
230000001900 immune effect Effects 0.000 claims description 21
239000004471 Glycine Substances 0.000 claims description 20
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 claims description 19
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238000002360 preparation method Methods 0.000 claims description 19
239000013598 vector Substances 0.000 claims description 19
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238000004587 chromatography analysis Methods 0.000 claims description 13
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229920002684 Sepharose Polymers 0.000 claims description 11
229920001184 polypeptide Polymers 0.000 claims description 10
238000000502 dialysis Methods 0.000 claims description 7
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239000000126 substance Substances 0.000 claims description 7
210000004962 mammalian cell Anatomy 0.000 claims description 6
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238000012258 culturing Methods 0.000 claims description 5
UREBDLICKHMUKA-CXSFZGCWSA-N dexamethasone Chemical compound C1CC2=CC(=O)C=C[C@]2(C)[C@]2(F)[C@@H]1[C@@H]1C[C@@H](C)[C@@](C(=O)CO)(O)[C@@]1(C)C[C@@H]2O UREBDLICKHMUKA-CXSFZGCWSA-N 0.000 claims description 5
229960003957 dexamethasone Drugs 0.000 claims description 5
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210000002540 macrophage Anatomy 0.000 claims description 5
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125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 claims description 3
241000193830 Bacillus <bacterium> Species 0.000 claims description 2
206010006187 Breast cancer Diseases 0.000 claims description 2
208000026310 Breast neoplasm Diseases 0.000 claims description 2
241000701959 Escherichia virus Lambda Species 0.000 claims description 2
241000238631 Hexapoda Species 0.000 claims description 2
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RLMISHABBKUNFO-WHFBIAKZSA-N Ala-Ala-Gly Chemical compound C[C@H](N)C(=O)N[C@@H](C)C(=O)NCC(O)=O RLMISHABBKUNFO-WHFBIAKZSA-N 0.000 claims 15
BYXHQQCXAJARLQ-ZLUOBGJFSA-N Ala-Ala-Ala Chemical compound C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(O)=O BYXHQQCXAJARLQ-ZLUOBGJFSA-N 0.000 claims 13
XVZCXCTYGHPNEM-UHFFFAOYSA-N Leu-Leu-Pro Natural products CC(C)CC(N)C(=O)NC(CC(C)C)C(=O)N1CCCC1C(O)=O XVZCXCTYGHPNEM-UHFFFAOYSA-N 0.000 claims 2
SSJMZMUVNKEENT-IMJSIDKUSA-N Ser-Ala Chemical compound OC(=O)[C@H](C)NC(=O)[C@@H](N)CO SSJMZMUVNKEENT-IMJSIDKUSA-N 0.000 claims 2
JAWGSPUJAXYXJA-IHRRRGAJSA-N Ser-Phe-Arg Chemical compound NC(N)=NCCC[C@@H](C(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CO)N)CC1=CC=CC=C1 JAWGSPUJAXYXJA-IHRRRGAJSA-N 0.000 claims 2
XVZCXCTYGHPNEM-IHRRRGAJSA-N (2s)-1-[(2s)-2-[[(2s)-2-amino-4-methylpentanoyl]amino]-4-methylpentanoyl]pyrrolidine-2-carboxylic acid Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(O)=O XVZCXCTYGHPNEM-IHRRRGAJSA-N 0.000 claims 1
102100027324 2-hydroxyacyl-CoA lyase 1 Human genes 0.000 claims 1
102000005606 Activins Human genes 0.000 claims 1
108010059616 Activins Proteins 0.000 claims 1
235000001674 Agaricus brunnescens Nutrition 0.000 claims 1
LSLIRHLIUDVNBN-CIUDSAMLSA-N Ala-Asp-Lys Chemical compound C[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](C(O)=O)CCCCN LSLIRHLIUDVNBN-CIUDSAMLSA-N 0.000 claims 1
KXEVYGKATAMXJJ-ACZMJKKPSA-N Ala-Glu-Asp Chemical compound C[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(O)=O KXEVYGKATAMXJJ-ACZMJKKPSA-N 0.000 claims 1
MPLOSMWGDNJSEV-WHFBIAKZSA-N Ala-Gly-Asp Chemical compound [H]N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(O)=O MPLOSMWGDNJSEV-WHFBIAKZSA-N 0.000 claims 1
MDNAVFBZPROEHO-DCAQKATOSA-N Ala-Lys-Val Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(O)=O MDNAVFBZPROEHO-DCAQKATOSA-N 0.000 claims 1
MDNAVFBZPROEHO-UHFFFAOYSA-N Ala-Lys-Val Natural products CC(C)C(C(O)=O)NC(=O)C(NC(=O)C(C)N)CCCCN MDNAVFBZPROEHO-UHFFFAOYSA-N 0.000 claims 1
NZGRHTKZFSVPAN-BIIVOSGPSA-N Ala-Ser-Pro Chemical compound C[C@@H](C(=O)N[C@@H](CO)C(=O)N1CCC[C@@H]1C(=O)O)N NZGRHTKZFSVPAN-BIIVOSGPSA-N 0.000 claims 1
BVLPIIBTWIYOML-ZKWXMUAHSA-N Ala-Val-Asp Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(O)=O)C(O)=O BVLPIIBTWIYOML-ZKWXMUAHSA-N 0.000 claims 1
OMSKGWFGWCQFBD-KZVJFYERSA-N Ala-Val-Thr Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H]([C@@H](C)O)C(O)=O OMSKGWFGWCQFBD-KZVJFYERSA-N 0.000 claims 1
ZDILXFDENZVOTL-BPNCWPANSA-N Ala-Val-Tyr Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O ZDILXFDENZVOTL-BPNCWPANSA-N 0.000 claims 1
WESHVRNMNFMVBE-FXQIFTODSA-N Arg-Asn-Asp Chemical compound C(C[C@@H](C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CC(=O)O)C(=O)O)N)CN=C(N)N WESHVRNMNFMVBE-FXQIFTODSA-N 0.000 claims 1
ZJBUILVYSXQNSW-YTWAJWBKSA-N Arg-Thr-Pro Chemical compound C[C@H]([C@@H](C(=O)N1CCC[C@@H]1C(=O)O)NC(=O)[C@H](CCCN=C(N)N)N)O ZJBUILVYSXQNSW-YTWAJWBKSA-N 0.000 claims 1
XWGJDUSDTRPQRK-ZLUOBGJFSA-N Asn-Ala-Ser Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CC(N)=O XWGJDUSDTRPQRK-ZLUOBGJFSA-N 0.000 claims 1
DMLSCRJBWUEALP-LAEOZQHASA-N Asn-Glu-Val Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C(C)C)C(O)=O DMLSCRJBWUEALP-LAEOZQHASA-N 0.000 claims 1
JEEFEQCRXKPQHC-KKUMJFAQSA-N Asn-Leu-Phe Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC1=CC=CC=C1)C(O)=O JEEFEQCRXKPQHC-KKUMJFAQSA-N 0.000 claims 1
YXVAESUIQFDBHN-SRVKXCTJSA-N Asn-Phe-Ser Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CO)C(O)=O YXVAESUIQFDBHN-SRVKXCTJSA-N 0.000 claims 1
NECWUSYTYSIFNC-DLOVCJGASA-N Asp-Ala-Phe Chemical compound OC(=O)C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 NECWUSYTYSIFNC-DLOVCJGASA-N 0.000 claims 1
UBPMOJLRVMGTOQ-GARJFASQSA-N Asp-His-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CC2=CN=CN2)NC(=O)[C@H](CC(=O)O)N)C(=O)O UBPMOJLRVMGTOQ-GARJFASQSA-N 0.000 claims 1
MJJIHRWNWSQTOI-VEVYYDQMSA-N Asp-Thr-Arg Chemical compound OC(=O)C[C@H](N)C(=O)N[C@@H]([C@H](O)C)C(=O)N[C@@H](CCCN=C(N)N)C(O)=O MJJIHRWNWSQTOI-VEVYYDQMSA-N 0.000 claims 1
PLOKOIJSGCISHE-BYULHYEWSA-N Asp-Val-Asn Chemical compound [H]N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(N)=O)C(O)=O PLOKOIJSGCISHE-BYULHYEWSA-N 0.000 claims 1
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JVSBYEDSSRZQGV-GUBZILKMSA-N Glu-Asp-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](N)CCC(O)=O JVSBYEDSSRZQGV-GUBZILKMSA-N 0.000 claims 1
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BRFJMRSRMOMIMU-WHFBIAKZSA-N Gly-Ala-Asn Chemical compound NCC(=O)N[C@@H](C)C(=O)N[C@@H](CC(N)=O)C(O)=O BRFJMRSRMOMIMU-WHFBIAKZSA-N 0.000 claims 1
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KEKTTYCXKGBAAL-VGDYDELISA-N Ile-His-Ser Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)N[C@@H](CO)C(=O)O)N KEKTTYCXKGBAAL-VGDYDELISA-N 0.000 claims 1
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SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
229930182823 kanamycin A Natural products 0.000 description 1
239000000787 lecithin Substances 0.000 description 1
229940067606 lecithin Drugs 0.000 description 1
235000010445 lecithin Nutrition 0.000 description 1
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230000004807 localization Effects 0.000 description 1
239000004325 lysozyme Substances 0.000 description 1
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235000010335 lysozyme Nutrition 0.000 description 1
238000010841 mRNA extraction Methods 0.000 description 1
UEGPKNKPLBYCNK-UHFFFAOYSA-L magnesium acetate Chemical compound [Mg+2].CC([O-])=O.CC([O-])=O UEGPKNKPLBYCNK-UHFFFAOYSA-L 0.000 description 1
239000011654 magnesium acetate Substances 0.000 description 1
235000011285 magnesium acetate Nutrition 0.000 description 1
229940069446 magnesium acetate Drugs 0.000 description 1
239000011159 matrix material Substances 0.000 description 1
230000001404 mediated effect Effects 0.000 description 1
230000001394 metastastic effect Effects 0.000 description 1
208000037819 metastatic cancer Diseases 0.000 description 1
208000011575 metastatic malignant neoplasm Diseases 0.000 description 1
206010061289 metastatic neoplasm Diseases 0.000 description 1
229930182817 methionine Natural products 0.000 description 1
HPNSFSBZBAHARI-UHFFFAOYSA-N micophenolic acid Natural products OC1=C(CC=C(C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-UHFFFAOYSA-N 0.000 description 1
230000000813 microbial effect Effects 0.000 description 1
230000005012 migration Effects 0.000 description 1
238000013508 migration Methods 0.000 description 1
230000004048 modification Effects 0.000 description 1
238000012986 modification Methods 0.000 description 1
230000004899 motility Effects 0.000 description 1
210000004877 mucosa Anatomy 0.000 description 1
229960000951 mycophenolic acid Drugs 0.000 description 1
HPNSFSBZBAHARI-RUDMXATFSA-N mycophenolic acid Chemical compound OC1=C(C\C=C(/C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-RUDMXATFSA-N 0.000 description 1
210000004897 n-terminal region Anatomy 0.000 description 1
239000006225 natural substrate Substances 0.000 description 1
230000009871 nonspecific binding Effects 0.000 description 1
231100000252 nontoxic Toxicity 0.000 description 1
230000003000 nontoxic effect Effects 0.000 description 1
102000039446 nucleic acids Human genes 0.000 description 1
108020004707 nucleic acids Proteins 0.000 description 1
150000007523 nucleic acids Chemical class 0.000 description 1
239000003921 oil Substances 0.000 description 1
229940092253 ovalbumin Drugs 0.000 description 1
YPZRWBKMTBYPTK-UHFFFAOYSA-N oxidized gamma-L-glutamyl-L-cysteinylglycine Natural products OC(=O)C(N)CCC(=O)NC(C(=O)NCC(O)=O)CSSCC(C(=O)NCC(O)=O)NC(=O)CCC(N)C(O)=O YPZRWBKMTBYPTK-UHFFFAOYSA-N 0.000 description 1
239000006174 pH buffer Substances 0.000 description 1
238000012856 packing Methods 0.000 description 1
230000036961 partial effect Effects 0.000 description 1
230000001575 pathological effect Effects 0.000 description 1
230000037361 pathway Effects 0.000 description 1
230000035515 penetration Effects 0.000 description 1
229940049954 penicillin Drugs 0.000 description 1
230000035699 permeability Effects 0.000 description 1
238000000819 phase cycle Methods 0.000 description 1
150000004633 phorbol derivatives Chemical class 0.000 description 1
239000002644 phorbol ester Substances 0.000 description 1
NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
239000010452 phosphate Substances 0.000 description 1
210000002826 placenta Anatomy 0.000 description 1
229940012957 plasmin Drugs 0.000 description 1
230000008488 polyadenylation Effects 0.000 description 1
229920002647 polyamide Polymers 0.000 description 1
235000011056 potassium acetate Nutrition 0.000 description 1
230000000069 prophylactic effect Effects 0.000 description 1
235000019833 protease Nutrition 0.000 description 1
238000002731 protein assay Methods 0.000 description 1
230000017854 proteolysis Effects 0.000 description 1
230000002797 proteolythic effect Effects 0.000 description 1
230000001105 regulatory effect Effects 0.000 description 1
238000011160 research Methods 0.000 description 1
230000004044 response Effects 0.000 description 1
230000000717 retained effect Effects 0.000 description 1
238000004007 reversed phase HPLC Methods 0.000 description 1
229940016590 sarkosyl Drugs 0.000 description 1
108700004121 sarkosyl Proteins 0.000 description 1
230000035945 sensitivity Effects 0.000 description 1
239000003001 serine protease inhibitor Substances 0.000 description 1
239000012679 serum free medium Substances 0.000 description 1
230000035939 shock Effects 0.000 description 1
239000010802 sludge Substances 0.000 description 1
239000000779 smoke Substances 0.000 description 1
239000001509 sodium citrate Substances 0.000 description 1
NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
FQENQNTWSFEDLI-UHFFFAOYSA-J sodium diphosphate Chemical compound [Na+].[Na+].[Na+].[Na+].[O-]P([O-])(=O)OP([O-])([O-])=O FQENQNTWSFEDLI-UHFFFAOYSA-J 0.000 description 1
KSAVQLQVUXSOCR-UHFFFAOYSA-M sodium lauroyl sarcosinate Chemical compound [Na+].CCCCCCCCCCCC(=O)N(C)CC([O-])=O KSAVQLQVUXSOCR-UHFFFAOYSA-M 0.000 description 1
229940048086 sodium pyrophosphate Drugs 0.000 description 1
239000007790 solid phase Substances 0.000 description 1
238000000527 sonication Methods 0.000 description 1
239000000600 sorbitol Substances 0.000 description 1
230000009870 specific binding Effects 0.000 description 1
230000004936 stimulating effect Effects 0.000 description 1
229960005322 streptomycin Drugs 0.000 description 1
238000006467 substitution reaction Methods 0.000 description 1
238000011477 surgical intervention Methods 0.000 description 1
230000002459 sustained effect Effects 0.000 description 1
210000001179 synovial fluid Anatomy 0.000 description 1
230000002194 synthesizing effect Effects 0.000 description 1
229940056501 technetium 99m Drugs 0.000 description 1
235000019818 tetrasodium diphosphate Nutrition 0.000 description 1
239000001577 tetrasodium phosphonato phosphate Substances 0.000 description 1
WROMPOXWARCANT-UHFFFAOYSA-N tfa trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F.OC(=O)C(F)(F)F WROMPOXWARCANT-UHFFFAOYSA-N 0.000 description 1
238000010257 thawing Methods 0.000 description 1
230000002537 thrombolytic effect Effects 0.000 description 1
210000001541 thymus gland Anatomy 0.000 description 1
101150031241 tos gene Proteins 0.000 description 1
239000003053 toxin Substances 0.000 description 1
231100000765 toxin Toxicity 0.000 description 1
108700012359 toxins Proteins 0.000 description 1
101150104391 traT gene Proteins 0.000 description 1
238000013518 transcription Methods 0.000 description 1
230000035897 transcription Effects 0.000 description 1
230000001131 transforming effect Effects 0.000 description 1
230000032258 transport Effects 0.000 description 1
229940108519 trasylol Drugs 0.000 description 1
QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
229960004319 trichloroacetic acid Drugs 0.000 description 1
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
PIEPQKCYPFFYMG-UHFFFAOYSA-N tris acetate Chemical compound CC(O)=O.OCC(N)(CO)CO PIEPQKCYPFFYMG-UHFFFAOYSA-N 0.000 description 1
210000004881 tumor cell Anatomy 0.000 description 1
230000002476 tumorcidal effect Effects 0.000 description 1
238000000108 ultra-filtration Methods 0.000 description 1
210000002700 urine Anatomy 0.000 description 1
210000003556 vascular endothelial cell Anatomy 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- 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
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/86—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving blood coagulating time or factors, or their receptors
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/81—Protease inhibitors
- C07K14/8107—Endopeptidase (E.C. 3.4.21-99) inhibitors
- C07K14/811—Serine protease (E.C. 3.4.21) inhibitors
- C07K14/8121—Serpins
- C07K14/8132—Plasminogen activator inhibitors
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/81—Protease inhibitors
- G01N2333/8107—Endopeptidase (E.C. 3.4.21-99) inhibitors
- G01N2333/811—Serine protease (E.C. 3.4.21) inhibitors
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/90—Enzymes; Proenzymes
- G01N2333/914—Hydrolases (3)
- G01N2333/948—Hydrolases (3) acting on peptide bonds (3.4)
- G01N2333/972—Plasminogen activators
- G01N2333/9723—Urokinase

Landscapes

Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Chemical & Material Sciences (AREA)
Engineering & Computer Science (AREA)
Organic Chemistry (AREA)
General Health & Medical Sciences (AREA)
Molecular Biology (AREA)
Medicinal Chemistry (AREA)
Hematology (AREA)
Biomedical Technology (AREA)
Biochemistry (AREA)
Genetics & Genomics (AREA)
Biotechnology (AREA)
Urology & Nephrology (AREA)
Immunology (AREA)
Physics & Mathematics (AREA)
Microbiology (AREA)
Biophysics (AREA)
Veterinary Medicine (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Zoology (AREA)
Wood Science & Technology (AREA)
Public Health (AREA)
Animal Behavior & Ethology (AREA)
Food Science & Technology (AREA)
Pharmacology & Pharmacy (AREA)
Analytical Chemistry (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
General Physics & Mathematics (AREA)
Pathology (AREA)
Gastroenterology & Hepatology (AREA)
General Chemical & Material Sciences (AREA)
Chemical Kinetics & Catalysis (AREA)
Cell Biology (AREA)
General Engineering & Computer Science (AREA)
Bioinformatics & Cheminformatics (AREA)
Pain & Pain Management (AREA)
Rheumatology (AREA)
Plant Pathology (AREA)
Peptides Or Proteins (AREA)

DK595187A 1986-03-13 1987-11-13 Fremgangsmåde til fremstilling af renset minactivin, minactivinkodende DNA-molekyle, rekombinant DNA-molekyle, sammensmeltet gen, vært, reagent til lokalisering og definering af grænserne for tumorer i histologiske prøver, samt anvendelse af det rekombinante DNA-molekyle, minactivinet og peptider deraf DK172400B1 (da)

Applications Claiming Priority (10)

Application Number	Priority Date	Filing Date	Title
AUPH501786		1986-03-13
AUPH501786		1986-03-13
AUPH603386		1986-05-22
AUPH603386		1986-05-22
AUPH810086		1986-09-18
AUPH810086		1986-09-18
AUPH910486		1986-11-21
AUPH910486		1986-11-21
PCT/AU1987/000068 WO1987005628A1 (fr)	1986-03-13	1987-03-13	Minactivine produite par la technique de l'adn recombinant
AU8700068		1987-03-13

Publications (3)

Publication Number	Publication Date
DK595187D0 DK595187D0 (da)	1987-11-13
DK595187A DK595187A (da)	1988-07-21
DK172400B1 true DK172400B1 (da)	1998-05-18

Family

ID=27424177

Family Applications (2)

Application Number	Title	Priority Date	Filing Date
DK595187A DK172400B1 (da)	1986-03-13	1987-11-13	Fremgangsmåde til fremstilling af renset minactivin, minactivinkodende DNA-molekyle, rekombinant DNA-molekyle, sammensmeltet gen, vært, reagent til lokalisering og definering af grænserne for tumorer i histologiske prøver, samt anvendelse af det rekombinante DNA-molekyle, minactivinet og peptider deraf
DK027097A DK27097A (da)	1986-03-13	1997-03-13	Minactivin og fremgangsmåde til fremstilling deraf

Family Applications After (1)

Application Number	Title	Priority Date	Filing Date
DK027097A DK27097A (da)	1986-03-13	1997-03-13	Minactivin og fremgangsmåde til fremstilling deraf

Country Status (13)

Country	Link
US (1)	US5426044A (fr)
EP (1)	EP0238275B1 (fr)
JP (2)	JP2589996B2 (fr)
KR (1)	KR960001820B1 (fr)
CN (2)	CN1032019C (fr)
AT (1)	ATE132192T1 (fr)
CA (1)	CA1338381C (fr)
DE (1)	DE3751646T2 (fr)
DK (2)	DK172400B1 (fr)
IL (1)	IL81879A (fr)
NO (1)	NO178504C (fr)
NZ (1)	NZ219608A (fr)
WO (1)	WO1987005628A1 (fr)

Families Citing this family (6)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US4923807A (en) *	1984-05-18	1990-05-08	New England Medical Center Hospitals Inc.	Arg-Serpin human plasminogen activator inhibitor designated PAI-2
ES2104610T3 (es) *	1989-09-05	1997-10-16	Biotech Australia Pty Ltd	Proceso para la preparacion de pai-2.
AU625018B2 (en) *	1989-12-20	1992-06-25	Biotech Australia Pty Limited	Variants of pai-2
GB9026737D0 (en) *	1990-12-08	1991-01-30	Delta Biotechnology Ltd	Cancer treatment
US5994309A (en)	1997-07-25	1999-11-30	Angstrom Pharmaceuticals, Inc.	Anti-invasive and anti-angiogenic compositions and methods
CN102586187A (zh) *	2012-02-23	2012-07-18	深圳市中美康士生物科技有限公司	一种中性粒细胞体外保存方法及培养基

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US4923807A (en) *	1984-05-18	1990-05-08	New England Medical Center Hospitals Inc.	Arg-Serpin human plasminogen activator inhibitor designated PAI-2
EP0192671B1 (fr) *	1984-08-13	1993-12-29	Biotechnology Australia Pty. Ltd.	Minactivin
CA1331355C (fr) *	1986-04-21	1994-08-09	Bioenterprises Pty. Ltd	Immunopotentialisation

1987
- 1987-03-12 IL IL8187987A patent/IL81879A/en not_active IP Right Cessation
- 1987-03-13 WO PCT/AU1987/000068 patent/WO1987005628A1/fr not_active Ceased
- 1987-03-13 AT AT87302200T patent/ATE132192T1/de not_active IP Right Cessation
- 1987-03-13 NZ NZ219608A patent/NZ219608A/en unknown
- 1987-03-13 CA CA000531981A patent/CA1338381C/fr not_active Expired - Fee Related
- 1987-03-13 KR KR1019870701038A patent/KR960001820B1/ko not_active Expired - Fee Related
- 1987-03-13 JP JP62501852A patent/JP2589996B2/ja not_active Expired - Fee Related
- 1987-03-13 EP EP87302200A patent/EP0238275B1/fr not_active Expired - Lifetime
- 1987-03-13 DE DE3751646T patent/DE3751646T2/de not_active Expired - Fee Related
- 1987-03-13 CN CN87102725A patent/CN1032019C/zh not_active Expired - Fee Related
- 1987-11-11 NO NO874704A patent/NO178504C/no not_active IP Right Cessation
- 1987-11-13 DK DK595187A patent/DK172400B1/da not_active IP Right Cessation
1991
- 1991-04-30 US US07/693,636 patent/US5426044A/en not_active Expired - Lifetime
1994
- 1994-05-21 CN CN94105143A patent/CN1100957A/zh active Pending
1995
- 1995-05-29 JP JP7153825A patent/JP2660681B2/ja not_active Expired - Fee Related
1997
- 1997-03-13 DK DK027097A patent/DK27097A/da not_active Application Discontinuation

Also Published As

Publication number	Publication date
EP0238275A3 (en)	1989-05-10
JP2660681B2 (ja)	1997-10-08
DK595187A (da)	1988-07-21
JPH08112094A (ja)	1996-05-07
NO178504B (no)	1996-01-02
ATE132192T1 (de)	1996-01-15
DK595187D0 (da)	1987-11-13
CN1032019C (zh)	1996-06-12
NZ219608A (en)	1991-05-28
KR880701073A (ko)	1988-07-25
WO1987005628A1 (fr)	1987-09-24
CA1338381C (fr)	1996-06-11
NO178504C (no)	1996-04-10
IL81879A (en)	1994-07-31
JP2589996B2 (ja)	1997-03-12
JPS63503354A (ja)	1988-12-08
CN87102725A (zh)	1987-11-11
EP0238275A2 (fr)	1987-09-23
EP0238275B1 (fr)	1995-12-27
US5426044A (en)	1995-06-20
DK27097A (da)	1997-03-13
NO874704L (no)	1987-11-11
CN1100957A (zh)	1995-04-05
NO874704D0 (no)	1987-11-11
KR960001820B1 (ko)	1996-02-05
DE3751646T2 (de)	1996-10-17
DE3751646D1 (de)	1996-02-08

Publication	Publication Date	Title
US4966849A (en)	1990-10-30	CDNA and genes for human angiogenin (angiogenesis factor) and methods of expression
Shaper et al.	1986	Bovine galactosyltransferase: identification of a clone by direct immunological screening of a cDNA expression library.
Metzger et al.	1988	The nucleotide sequence and characterization of the relA gene of Escherichia coli.
MAURER‐FOGY et al.	1988	Cloning and expression of cDNA for human vascular anticoagulant, a Ca2+‐dependent phospholipid‐binding protein
US5872218A (en)	1999-02-16	Human platelet-derived growth factor receptor extracellular domain antibodies
JP3156082B2 (ja)	2001-04-16	マトリックスメタロプロテイナーゼ阻害剤ペプチド
JP2002186487A (ja)	2002-07-02	ファクターｖｉｉｉｃ組成物
JPH0272896A (ja)	1990-03-13	オンコスタチン―ａに対して特異的なモノクローナル抗体
CA1341516C (fr)	2006-11-28	Preparation du facteur x111a par manipulation genetique
EP0330396B1 (fr)	1995-06-21	Séquences d'ADN, molécules d'ADN recombinantes et procédés pour la production des lipocortins III, IV, V, et VI
JPH0866194A (ja)	1996-03-12	ヒト腫瘍壊死因子ミューテインをコードする遺伝子
JP2000074922A (ja)	2000-03-14	シュードモナス・アエルギノザの外部膜タンパク質ｆ
DK172400B1 (da)	1998-05-18	Fremgangsmåde til fremstilling af renset minactivin, minactivinkodende DNA-molekyle, rekombinant DNA-molekyle, sammensmeltet gen, vært, reagent til lokalisering og definering af grænserne for tumorer i histologiske prøver, samt anvendelse af det rekombinante DNA-molekyle, minactivinet og peptider deraf
KR100270348B1 (ko)	2000-12-01	전사인자 에이피알에프
JPH0787789B2 (ja)	1995-09-27	リポコルチンをコードするｄｎａ分子および形質転換宿主
AU645055B2 (en)	1994-01-06	Covalent angiogenin/RNase hybrids
US5270204A (en)	1993-12-14	Covalent angiogenin/RNase hybrids
US4950646A (en)	1990-08-21	DNA sequences, recombinant DNA molecules and processes for producing human lipocortin-like polypeptides
JPH03164179A (ja)	1991-07-16	Ｔｎｆレセプター、ｔｎｆ結合たん白質およびこれらをコードするｄｎａ
AU608752B2 (en)	1991-04-18	Minactivin produced by recombinant dna technology
WO1995011695A1 (fr)	1995-05-04	Sequence d'adn codant un polypeptide a proprietes anti-tumorales
JP2623807B2 (ja)	1997-06-25	セリンプロテアーゼおよびセリンプロテアーゼ遺伝子
CN100480264C (zh)	2009-04-22	一种广谱抑制癌细胞生长的蚯蚓蛋白及其编码序列
CA2166872A1 (fr)	1995-01-19	Gene de la glycoproteine v plaquettaire et applications
JPH0757192B2 (ja)	1995-06-21	新規なｄｎａ

Legal Events

Date	Code	Title	Description
1988-08-15	ATS	Application withdrawn
1988-09-05	AHS	Application shelved for other reasons than non-payment
1988-11-07	AHS	Application shelved for other reasons than non-payment
1989-03-13	AHS	Application shelved for other reasons than non-payment
1989-04-17	AHS	Application shelved for other reasons than non-payment
1989-08-07	AHS	Application shelved for other reasons than non-payment
1990-08-20	AHB	Application shelved due to non-payment
1990-10-01	AGE	Re-establishment of rights: approved
1998-05-18	B1	Patent granted (law 1993)
2003-10-27	PBP	Patent lapsed	Country of ref document: DK