Open AccessSensitivity to Ampicillin and Cephalothin of Enzymes Involved in Wall Peptide Crosslinking in Escherichia coli K12, Strain 44
Author(s) -
NguyenDistèche Martine,
Pollock Jerry J.,
Ghuysen JeanMarie,
Puig Juan,
Reynolds Peter,
Perkins Harold R.,
Coyette Jacques,
Salton Milton R. J.
Publication year - 1974
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1974.tb03287.x
Subject(s) - escherichia coli , ampicillin , enzyme , strain (injury) , endopeptidase , chemistry , carboxypeptidase , peptide , biochemistry , aminopeptidase , membrane , chromatography , microbiology and biotechnology , biology , leucine , amino acid , antibiotics , gene , anatomy
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.