Two Kinds of Neutral Serine Proteinases in Salted Muscle of Anchovy,Engraulis japonica
| Autor: | Nobuko Sugiyama, Fumio Nagayama, Mariko Sato, Masami Ishida |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Serine Proteinase Inhibitors
Molecular Sequence Data Sodium Chloride Applied Microbiology and Biotechnology Biochemistry Japonica Substrate Specificity Analytical Chemistry Mice Hydrolysis Enzyme Stability medicine Animals Humans Amino Acid Sequence Molecular Biology Peptide sequence chemistry.chemical_classification Sequence Homology Amino Acid biology Tetrapeptide Muscles Serine Endopeptidases Organic Chemistry Fishes Temperature General Medicine Hydrogen-Ion Concentration biology.organism_classification Trypsin Enzyme chemistry Anchoa Salted fish Biotechnology medicine.drug |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 59:1107-1112 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1271/bbb.59.1107 |
| Popis: | Two kinds of proteinases, type-I and type-II, were purified or partially purified from salted muscle of anchovy, Engraulis japonica. Mol. wts. of type-I and type-II proteinases were estimated to 25,000 and 37,000, respectively, on electrophoretic analysis. Both proteinases strongly hydrolyzed synthetic tri or tetrapeptide substrates specific to trypsin, alpha-thrombin, and an activated protein C, while they hardly hydrolyzed Arg-MCA and benzoyl Arg-MCA derivatives. The proteinases were inhibited by common trypsin inhibitors. Optimal pH for the proteinase activities were pH 6.8 (type-I) and pH 7.0 to 7.5 (type-II), and the proteinases showed the highest activities at 45 degrees C (type-I) and 50 degrees C (type-II). The N-terminal amino acid sequence of type-I proteinase, 1I-2V-3G-4G ... (29 residues were identified), was significantly similar to sequences of trypsins and tryptases. Based on these findings, both proteinases were presumed to be kinds of tryptases in E. japonica muscle. |
| Databáze: | OpenAIRE |
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