Affinity purification of endothia protease with a novel renin inhibitor SQ 32,970
Autor: | Tamara Dejneka, Deborah K. Little, Charles A. Free, Helen Weber, Denis E. Ryono, Jon A. Norman |
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Rok vydání: | 1989 |
Předmět: |
medicine.drug_class
medicine.medical_treatment Biophysics Biochemistry Renin inhibitor Substrate Specificity Sepharose Fungal Proteins Affinity chromatography Ascomycota Endopeptidases Renin medicine Aspartic Acid Endopeptidases Protease Inhibitors Molecular Biology Chromatography High Pressure Liquid chemistry.chemical_classification Fungal protein Chromatography Protease biology Hydrolysis Cell Biology Endothia biology.organism_classification Molecular Weight Kinetics Enzyme chemistry Enzyme inhibitor biology.protein Oligopeptides |
Zdroj: | Biochemical and biophysical research communications. 161(1) |
ISSN: | 0006-291X |
Popis: | A novel tripeptidic renin inhibitor is described, SQ 32,970, that will potently inhibit endothia protease. This inhibitor can be coupled to Sepharose and will allow the affinity-purification of endothia protease in one step to greater than 95% purity as measured by SDS PAGE. The purified endothia protease cleaves the Lys-Pro-Ala-Glu-Phe-Nph-Arg-Leu substrate at the Phe-Nph bond with a Kcat/Km of 7445 (s-1 mM-1) at pH 3.1 and 4057 (s-1 mM-1) at pH 6.0. Affinity purified endothia protease can be crystallized in the pH range in which it is enzymatically active and can be inhibited by renin inhibitors. |
Databáze: | OpenAIRE |
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