Preparation by direct metal exchange and kinetic study of active site metal substituted class I and class II Clostridium histolyticum collagenases
- 1 September 1988
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 27 (19) , 7413-7418
- https://doi.org/10.1021/bi00419a036
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 9 references indexed in Scilit:
- Preparation and reconstitution with divalent metal ions of class I and class II Clostridium histolyticum apocollagenasesBiochemistry, 1988
- Studies on the stimulation of the bacterial, collagenolytic enzyme clostridiopeptidase a by cobalt (ii) ionsInternational Journal of Biochemistry, 1986
- Spectral and kinetic studies of metal-substituted Aeromonas aminopeptidase: nonidentical, interacting metal-binding sitesBiochemistry, 1985
- The functional role of zinc in angiotensin converting enzyme: implications for the enzyme mechanismJournal of Inorganic Biochemistry, 1985
- Relationship between the individual collagenases of Clostridium histolyticum: evidence for evolution by gene duplicationBiochemistry, 1984
- Purification and separation of individual collagenases of Clostridium histolyticum using red dye ligand chromatographyBiochemistry, 1984
- Kinetics of carboxypeptidase A. I. Hydrolysis of carbobenzoxyglycyl-L-phenylalanine, benzoylglycyl-L-phenylalanine, and hippuryl-DL-.beta.-phenyllactic acid by metal-substituted and acetylated carboxypeptidasesBiochemistry, 1968
- Kinetic Studies on the Action of CollagenaseThe Journal of Biochemistry, 1965
- Metallocarboxypeptidases: Stability Constants and Enzymatic CharacteristicsJournal of Biological Chemistry, 1961