Open AccessSolubilization and Isolation of the Membrane‐Bound dd ‐Carboxypeptidase of Streptococcus faecalis ATCC 9790
Author(s) -
COYETTE Jacques,
GHUYSEN JeanMarie,
FONTANA Roberta
Publication year - 1978
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1978.tb12450.x
Subject(s) - enzyme , carboxypeptidase , penicillin , enterococcus faecalis , biochemistry , chemistry , streptococcus , solubilization , gel electrophoresis , bacteria , chromatography , biology , microbiology and biotechnology , escherichia coli , antibiotics , genetics , gene
Streptococcus faecalis ATCC 9790 possesses six membrane‐bound, penicillin‐binding proteins. That numbered 6 ( M r 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.