Ishiura et al., 1982 - Google Patents
Purification of an endogenous 68000-dalton inhibitor of ca2+-activated neutral protease from chicken skeletal muscleIshiura et al., 1982
- Document ID
- 12546096501315355316
- Author
- Ishiura S
- Tsuji S
- Murofushi H
- Suzuki K
- Publication year
- Publication venue
- Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology
External Links
Snippet
An endogenous inhibitor of Ca 2+-activated neutral protease has been purified from chicken skeletal muscle. The inhibitor, which was isolated by acid treatment and four subsequent chromatographic procedures, is a protein composed of a single polypeptide having a …
- 230000002401 inhibitory effect 0 title abstract description 113
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
- 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)
-
- 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)
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Ishiura et al. | Purification of an endogenous 68000-dalton inhibitor of ca2+-activated neutral protease from chicken skeletal muscle | |
Lenney et al. | Thermostable endogenous inhibitors of cathepsins B and H | |
Orlowski et al. | A soluble metalloendopeptidase from rat brain: purification of the enzyme and determination of specificity with synthetic and natural peptides | |
Rodis et al. | Naturally occurring protein crystals in the potato: inhibitor of papain, chymopapain, and ficin | |
原研治 et al. | Purification and characterization of cathepsin B from carp ordinary muscle. | |
ONO et al. | Rat pancreatic phospholipase A2: purification, characterization, and N-terminal amino acid sequence | |
Brockbank et al. | Purification and preliminary characterization of two asclepains from the latex of Asclepias syriaca L.(milkweed) | |
Capiralla et al. | Purification and characterization of a hydrophobic amino acid—specific endopeptidase from Halobacterium halobium S9 with potential application in debittering of protein hydrolysates | |
Nelson et al. | Extracellular acid and alkaline proteases from Candida olea | |
Weissenberg et al. | Species specific sensitivity towards the hemorrhagin of Ophiophagus hannah (Elapidae) | |
McDermott et al. | Purification and Characterization of Two Soluble C1−‐Activated Arginyl Aminopeptidases from Human Brain and Their Endopeptidase Action on Neuropeptides | |
Waters et al. | Purification and characterization of an iminopeptidase from the primary leaf of wheat (Triticum aestivum L.) | |
Moriyama et al. | Porcine liver succinyltrialanine p-nitroanilide hydrolytic enzyme. Its purification and characterization as a post-proline cleaving enzyme | |
Zolfaghari et al. | A multicatalytic high-molecular-weight neutral endopeptidase from human kidney | |
Chen et al. | Deoxyribonuclease of Syncephalastrum racemosum-enzymatic properties and molecular structure | |
Okada et al. | Alkaline phosphatase isozymes in the midgut of silkworm: purification of high pH-stable microvillus and labile cytosolic enzymes | |
Abe et al. | Purification and characterization of a cysteine proteinase inhibitor from the endosperm of corn | |
Manonmani et al. | Purification and properties of an extracellular proteinase of Trichoderma koningii | |
Muto et al. | Purification and characterization of rat pepsinogens whose contents increase with developmental progress | |
Paiva et al. | Purification and primary structure determination of two Bowman–Birk type trypsin isoinhibitors from Cratylia mollis seeds | |
Nishida et al. | Isolation and properties of two phospholipases A2 from the venom of an Australian elapid snake (Pseudechis australis) | |
Ikeda et al. | Purification and properties of the trypsin inhibitors from buckwheat seed | |
D'Aniello et al. | Peptidyl-D-amino acid hydrolase from Loligo vulgaris Lam. Purification and characterization. | |
IsHiDA et al. | Characteristics of psychrophilic alkaline phosphatase | |
DRYJANSKI et al. | Serine proteinase from Cucurbita ficifolia seed; purification, properties, substrate specificity and action on native squash trypsin inhibitor (CMTI I) |