Matsubara, 1970 - Google Patents
[46] Purification and assay of thermolysinMatsubara, 1970
- Document ID
- 11482111874300915437
- Author
- Matsubara H
- Publication year
- Publication venue
- Methods in enzymology
External Links
Snippet
Conclusion Clostripain is a unique enzyme with regard to its specificity. This property may be of advantage in protein sequence work where large initial peptide fragments are desired as well as in active site studies regarding the origin of its arginine specificity. The stringent …
- 108090001109 Thermolysin 0 title description 37
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)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6427—Chymotrypsins (3.4.21.1; 3.4.21.2); Trypsin (3.4.21.4)
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES OR MICRO-ORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/34—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving hydrolase
- C12Q1/37—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving hydrolase involving peptidase or proteinase
-
- 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
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/814—Enzyme separation or purification
- Y10S435/816—Enzyme separation or purification by solubility
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Matsubara | [46] Purification and assay of thermolysin | |
Matsuzawa et al. | Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT‐1 | |
Keay et al. | Proteases of the genus Bacillus. II. Alkaline proteases | |
Morihara et al. | Comparison of the specificities of various serine proteinases from microorganisms | |
Castellino et al. | [29] Human plasminogen | |
Prescott et al. | [44] Aeromonas aminopeptidase | |
Kim et al. | A fibrinolytic metalloprotease from the fruiting bodies of an edible mushroom, Armillariella mellea | |
Morita et al. | Purification and properties of prothrombin activator from the venom of Echis carinatus | |
Hofmann et al. | Blood coagulation induced by the venom of bot hrops atrox. 1. Identification, purification, and properties of a prothrombin activator | |
Cheung et al. | A soluble aspartate aminopeptidase from dog kidney | |
Uchikoba et al. | Cleavage specificity of cucumisin, a plant serine protease | |
Tsuru et al. | Purification and characterization of L-pyrrolidonecarboxylate peptidase from Bacillus amyloliquefaciens | |
Loewy et al. | Purification and characterization of a novel zinc-proteinase from cultures of Aeromonas hydrophila. | |
Gnosspelius | Purification and properties of an extracellular protease from Myxococcus virescens | |
Morihara et al. | Specificity of proteinase K from Tritirachium album Limber for synthetic peptides | |
Tsu et al. | The substrate specificity of Uca pugilator collagenolytic serine protease 1 correlates with the bovine type I collagen cleavage sites. | |
Markland Jr | [19] Crotalase | |
Davidson et al. | Aspergillus oryzae acid proteinase. Purification and properties, and formation of π-chymotrypsin | |
Mitchell et al. | 19 Glostripain | |
Teng et al. | Purification and properties of the main coagulant and anticoagulant principles of Vipera Russell II snake venom | |
Terashita et al. | Streptomyces pepsin inhibitor-insensitive carboxyl proteinase from Ganoderma lucidum | |
Gaucher et al. | [34] Thermomycolin | |
Oda et al. | Purification and properties of a proteinaceous metallo-proteinase inhibitor from Streptomyces nigrescens TK-23 | |
Hanada et al. | The isolation of collagenase and its enzymological and physico-chemical properties | |
Zolfaghari et al. | A high-molecular-mass neutral endopeptidase-24.5 from human lung |