Bacterial elastase. I. Isolation, purification and properties
Autor: | Betty B. Cohen, Ines Mandl |
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Rok vydání: | 1960 |
Předmět: |
chemistry.chemical_classification
Pancreatic Elastase Hydrolases Ph optimum Serine Endopeptidases Kinetics Elastase Biophysics Biology Isolation (microbiology) Flavobacterium Biochemistry Elastase I Microbiology Enzyme chemistry Proteinase activity Molecular Biology Pancreatic elastase Peptide Hydrolases |
Zdroj: | Archives of Biochemistry and Biophysics. 91:47-53 |
ISSN: | 0003-9861 |
DOI: | 10.1016/0003-9861(60)90453-7 |
Popis: | A bacterial elastase has been isolated from a flavobacterium species and freed from contaminating peptidase and unspecific proteinase activity. Some properties of this new enzyme, such as pH, stability, effect of metals and other potential inhibitors, kinetics, and specificity are described. The bacterial enzyme is more specific than pancreatic elastase, has a lower pH optimum, and is not affected by 1% NaCl and serum inhibitors. |
Databáze: | OpenAIRE |
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