De Caro et al., 1998 - Google Patents
An enzymatically active truncated form (− 55 N-terminal residues) of rabbit gastric lipase. Correlation between the enzymatic activity and disulfide bond oxydo …De Caro et al., 1998
- Document ID
- 10184231867417823847
- Author
- De Caro J
- Verger R
- De Caro A
- Publication year
- Publication venue
- Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology
External Links
Snippet
Rabbit gastric lipase (RGL) was subjected to proteolysis with trypsin and led to cleavage occurring at three defined sites (Lys-4, Arg-55 and Arg-229). The tryptic hydrolysate contained four fragments: Gly-230-Lys-379 (T1), Gly-56-Arg-229 (T2), Ser-5-Arg-55 (T3), as …
- 101700033034 LIPF 0 title abstract description 51
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
- C12N9/18—Carboxylic ester hydrolases (3.1.1)
- C12N9/20—Triglyceride splitting, e.g. by means of lipase
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
- C12N9/52—Proteinases Endopeptidases (3.4.21-3.4.25) derived from bacteria
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL, OR TOILET PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/43—Enzymes; Proenzymes; Derivatives thereof
- A61K38/46—Hydrolases (3)
- A61K38/465—Hydrolases (3) acting on ester bonds (3.1), e.g. lipases, ribonucleases
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/40—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against enzymes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y301/00—Hydrolases acting on ester bonds (3.1)
- C12Y301/01—Carboxylic ester hydrolases (3.1.1)
- C12Y301/01004—Phospholipase A2 (3.1.1.4)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Carriere et al. | Purification and biochemical characterization of dog gastric lipase | |
| Lowe et al. | Cloning and characterization of human pancreatic lipase cDNA | |
| Abouakil et al. | Purification of pancreatic carboxylic-ester hydrolase by immunoaffinity and its application to the human bile-salt-stimulated lipase | |
| Gargouri et al. | Studies on the inhibition of pancreatic and microbial lipases by soybean proteins. | |
| Ono et al. | Purification and characterization of a membrane-associated phospholipase A2 from rat spleen. Its comparison with a cytosolic phospholipase A2 S-1. | |
| Whitcomb et al. | Human pancreatic digestive enzymes | |
| Stafforini et al. | Mammalian platelet-activating factor acetylhydrolases | |
| Wong et al. | Lipoprotein lipase domain function. | |
| Savel'ev et al. | Amylolytic activity of IgG and sIgA immunoglobulins from human milk | |
| Aloulou et al. | A comparative study on two fungal lipases from Thermomyces lanuginosus and Yarrowia lipolytica shows the combined effects of detergents and pH on lipase adsorption and activity | |
| Bougatef et al. | Pepsinogen and pepsin from the stomach of smooth hound (Mustelus mustelus): Purification, characterization and amino acid terminal sequences | |
| De Caro et al. | Pancreatic lipase-related protein 1 (PLRP1) is present in the pancreatic juice of several species | |
| Riley et al. | Pancreatic cholesterol esterases. 2. Purification and characterization of human pancreatic fatty acid ethyl ester synthase | |
| JP2514167B2 (en) | Polypeptides and polypeptide compositions | |
| Johnston et al. | Isolation and characterization of a trypsin from the slipper lobster, Thenus orientalis (Lund) | |
| AU727469B2 (en) | Specific pancreatic lipase inhibitors and their applications | |
| De Caro et al. | Purification and molecular characterization of lamb pregastric lipase | |
| Sayari et al. | Characterization of turkey pancreatic lipase | |
| Zouari et al. | Purification and characterization of a novel lipase from the digestive glands of a primitive animal: the scorpion | |
| Venkatesh et al. | The flavin-containing monooxygenase of mouse kidney: A comparison with the liver enzyme | |
| De Caro et al. | An enzymatically active truncated form (− 55 N-terminal residues) of rabbit gastric lipase. Correlation between the enzymatic activity and disulfide bond oxydo-reduction state | |
| Abousalham et al. | Uncoupling of catalysis and colipase binding in pancreatic lipase by limited proteolysis | |
| Tan | Isolation and characterization of the thrombin-like enzyme from Cryptelytrops purpureomaculatus venom | |
| Spilburg et al. | Identification of a species specific regulatory site in human pancreatic cholesterol esterase | |
| Mikhailova et al. | Autolysis of bovine enteropeptidase heavy chain: evidence of fragment 118–465 involvement in trypsinogen activation |