Naphthylamidase Activity of Leptospira
| Autor: | Goldberg Hs, D. C. Blenden, Glenna C. Burton |
|---|---|
| Rok vydání: | 1970 |
| Předmět: |
Naphthalenes
Aminopeptidases Aminopeptidase General Biochemistry Genetics and Molecular Biology Microbiology Leucyl Aminopeptidase Leucine Leptospira Enzymatic hydrolysis Serotyping General Pharmacology Toxicology and Pharmaceutics Leucyl aminopeptidase Metabolism and Products Alanine chemistry.chemical_classification General Immunology and Microbiology biology Temperature General Medicine Hydrogen-Ion Concentration biology.organism_classification Enzyme assay Culture Media Enzyme chemistry Biochemistry Spectrophotometry biology.protein Colorimetry |
| Zdroj: | Applied Microbiology. 19:586-588 |
| ISSN: | 0003-6919 |
| DOI: | 10.1128/am.19.4.586-588.1970 |
| Popis: | Extracts of 18 serotypes of the genus Leptospira were found to possess naphthylamidase activity, and differences in the pathogenic and saprophytic strains were noted. The former exhibited a preference for the leucyl naphthylamide substrate, whereas the latter demonstrated greater hydrolysis of alanyl naphthylamide. With the leucyl naphthylamide as substrate, pathogenic strains showed 10 to 20 times higher naphthylamidase activity than saprophytic strains. Optimal temperature and p H for enzymatic hydrolysis also differed between pathogenic and saprophytic strains. Maximal enzymatic activities for pathogenic and saprophytic naphthylamidases were 41 and 37 C, respectively, at p H 8.0 to 8.5. The p H and temperature optima suggested that the leptospiral enzyme activity was not leucine aminopeptidase. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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