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Solubilization and Isolation of the Membrane-Bound dd-Carboxypeptidase of Streptococcus faecalis ATCC 9790
Properties of the Purified Enzyme
Article first published online: 28 JUN 2008
DOI: 10.1111/j.1432-1033.1978.tb12450.x
1742-4658/asset/cover.gif?v=1&s=fc98a9fc84ccc5e1b83463cabb40f397544364eb "European Journal of Biochemistry")
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How to Cite
COYETTE, J., GHUYSEN, J.-M. and FONTANA, R. (1978), Solubilization and Isolation of the Membrane-Bound dd-Carboxypeptidase of Streptococcus faecalis ATCC 9790. European Journal of Biochemistry, 88: 297–305. doi: 10.1111/j.1432-1033.1978.tb12450.x
Publication History
- Issue published online: 28 JUN 2008
- Article first published online: 28 JUN 2008
- (Received January 25, 1978)
- Abstract
- Article
- References
- Cited By
Streptococcus faecalis ATCC 9790 possesses six membrane-bound, penicillin-binding proteins. That numbered 6 (Mr 43000) is the most abundant one and is the dd-carboxypeptidase studied previously. The enzyme has been solubilized and purified to the stage where one single protein band can be detected by gel electrophoresis. The purification procedure does not alter the properties that the enzyme exhibits when it is membrane-bound. The dd-carboxypeptidase itself may be a killing target for penicillin in S. faecalis.