ORBi: Nguyen-Distèche Martine - Sensitivity to ampicillin and cephalothin of enzymes involved in wall peptide crosslinking in Escherichia coli K12, strain 44

Reference : Sensitivity to ampicillin and cephalothin of enzymes involved in wall peptide crosslinki...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Microbiology Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/83094

Title :	Sensitivity to ampicillin and cephalothin of enzymes involved in wall peptide crosslinking in Escherichia coli K12, strain 44
Language :	English
Author, co-author :	Nguyen-Distèche, Martine [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > >]
	Pollock, Jerry J. [New York University School of Medicine > Department of Microbiology > > >]
	Ghuysen, Jean-Marie [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > > >]
	Puig, Juan [Universitad de Los Andes > Faculdad de Ciencia > Departamento de Biologia > >]
	Reynolds, Peter [University of Cambridge > Department of Biochemistry > Sub-Department of Chemical Microbiology > >]
	Perkins, Harnold-R. [University of Cambridge > Department of Biochemistry > Sub-Department of Chemical Microbiology > >]
	Coyette, Jean [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > > >]
	Salton, Milton-R-J. [National Institute for Medical Research > > > > >]
Publication date :	1-Feb-1974
Journal title :	European Journal of Biochemistry
Publisher :	Blackwell Science
Volume :	41
Issue/season :	3
Pages :	457-463
Audience :	International
ISSN :	0014-2956
e-ISSN :	1432-1033
City :	Oxford
Country :	United Kingdom
Keywords :	[en] acyltransferases metabolism ; ampicillin pharmacology ; bacterial proteins biosynthesis ; carboxypeptidases metabolism ; cell membrane enzymology ; cell wall/metabolism ; cephalothin pharmacology ; dose-response relationship, drug ; escherichia coli/cytology/drug effects enzymology ; tethal dose 50 ; microscopy, phase-contrast ; mutation ; nitrosoguanidines/pharmacology ; penicillin g/pharmacology ; penicillinase/metabolism ; peptide hydrolases/*metabolism ; rifampin/pharmacology ; surface-active agents
Abstract :	[en] After extraction of the membranes of Escherichia coli K12 strain 44 by Brij-36T, each of the four enzyme activities (natural transpeptidase, unnatural transpeptidase, carboxypeptidase and endopeptidase) of the wall peptide crosslinking system, occurs in two forms characterized by large differences in their sensitivity to ampicillin (but much smaller differences in their sensitivity to cephalothin). The fractionation of the enzyme activities into two groups of low and high sensitivity to ampicillin is achieved essentially by chromatography of the membrane extract on DEAE-cellulose.
Funders :	Fonds de la Recherche Fondamentale Collective
Target :	Researchers ; Professionals
Permalink :	http://hdl.handle.net/2268/83094
DOI :	10.1111/j.1432-1033.1974.tb03287.x

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