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Solubilization and isolation of the membrane-bound dd-carboxypeptidase of Streptococcus faecalis ATCC 9790

Coyette, Jaques and Ghuysen, Jean-Marie and Fontana, Roberta (1978) Solubilization and isolation of the membrane-bound dd-carboxypeptidase of Streptococcus faecalis ATCC 9790. European Journal of Biochemistry, Vol. 88 (1), p. 297-305. eISSN 1432-1033. Article.

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Abstract

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.

Item Type:Article
ID Code:1275
Status:Published
Refereed:Yes
Uncontrolled Keywords:Streptococcus faecalis ATCC 9790, membrane-bound, enzyme activities
Subjects:Area 06 - Scienze mediche > MED/07 Microbiologia e microbiologia clinica
Divisions:001 Università di Sassari > 01 Dipartimenti > Scienze biomediche
Publisher:Blackwell Science on behalf of the Federation of European Biochemical Societies / Wiley
eISSN:1432-1033
Deposited On:18 Aug 2009 10:04

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