Reference : Isolation of the membrane-bound 26 000-Mr penicillin-binding protein of Streptomyces ...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/83022
Isolation of the membrane-bound 26 000-Mr penicillin-binding protein of Streptomyces strain K15 in the form of a penicillin-sensitive D-alanyl-D-alanine-cleaving transpeptidase
English
Nguyen-Distèche, Martine mailto [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > >]
Leyh-Bouille, Mélina [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie > Service de Microbiologie > > >]
1-Oct-1982
Biochemical Journal
Portland Press
207
1
109-115
Yes (verified by ORBi)
International
0264-6021
1470-8728
London
United Kingdom
[en] bacterial proteins ; carboxypeptidases/*isolation & purification ; carrier proteins/*isolation & purification/metabolism ; cell membrane/enzymology ; cetrimonium compounds ; chromatography, affinity ; chromatography, gel ; detergents ; electrophoresis, polyacrylamide gel ; hexosyltransferases ; muramoylpentapeptide carboxypeptidase/antagonists & inhibitors/*isolation ; purification/metabolism ; penicillin g/*pharmacology ; penicillin-binding proteins ; peptidyl transferases ; streptomyces/*enzymology
[en] The membrane-bound, 26 000-Mr penicillin-binding protein of Streptomyces K15 has been isolated in the form of an effective, penicillin-sensitive D-alanyl-D-alanine-cleaving peptidase exhibiting high transpeptidase activity (greater than 95%) and very low carboxy-peptidase activity (less than 5%). The penicillin-binding protein/transpeptidase can be extracted directly from the mycelium with N-cetyl-NNN-trimethylammonium bromide (Cetavlon) and subsequently obtained at 90% purity and with an 8000-fold specific enrichment (when compared with the activity of the isolated membranes) by a two-step procedure involving Sephadex filtration and affinity chromatography on ampicillin-linked CH Sepharose 4B in the presence of detergent. At saturating concentrations of the co-substrates diacetyl-L-Lys-D-Ala-D-Ala and Gly-Gly, the catalytic-centre activity is about 0.3 s-1.
Fonds de la Recherche Scientifique Médicale - FRSM ; National Institutes of Health - NIH
Researchers ; Professionals
http://hdl.handle.net/2268/83022

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