Reference : Solubilization and isolation of the membrane-bound DD-carboxypeptidase of Streptococcus ...
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/83043
Solubilization and isolation of the membrane-bound DD-carboxypeptidase of Streptococcus faecalis ATCC9790. Properties of the purified enzyme
English
Coyette, Jacques [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > > >]
Fontana, Roberta [Universita di Sassari > Istituto di Microbiologia > > >]
17-Jul-1978
European Journal of Biochemistry
Blackwell Science
88
1
297-305
Yes (verified by ORBi)
International
0014-2956
1432-1033
Oxford
United Kingdom
[en] carboxypeptidases/*metabolism ; carrier proteins/isolation & purification ; cell membrane/*enzymology ; cloxacillin/metabolism ; enterococcus faecalis/drug effects/*enzymology ; muramoylpentapeptide carboxypeptidase/isolation & purification/*metabolism ; oligopeptides/metabolism ; penicillin g/metabolism ; penicillins/metabolism ; solubility
[en] 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.
Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS ; National Institutes of Health - NIH
Researchers ; Professionals
http://hdl.handle.net/2268/83043

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