Reference : Fractionation of the DD-carboxypeptidase-transpeptidase activities solubilized from memb...
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/83100
Fractionation of the DD-carboxypeptidase-transpeptidase activities solubilized from membranes of Escherichia coli K12, strain 44
English
Pollock, Jerry J. [New York University School of Medecine > Department of Microbiology > > >]
Nguyen-Disteche, Martine [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 > > >]
Coyette, Jacques mailto [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > >]
Linder, Régina [New York University School of Medicin > Department of Microbiology > > > >]
Salton, Milton R. [New York University School of Medicin > Department of Microbiology > > >]
Kim, Kwang S. [New York University School of Medicine > Department of Microbiology > > >]
Perkins, Harold-R [M. R. C. National Institute for Medical Research > > > > > >]
Reynolds, Peter [University of Cambridge > Sub-Department of Chemical Microbiology > > >]
1974
European Journal of Biochemistry
Blackwell Science
41
3
439-446
Yes (verified by ORBi)
International
0014-2956
1432-1033
Oxford
United Kingdom
[en] ccyltransferases/*isolation & purification/metabolism ; alanine ; ampicillin ; carbon radioisotopes ; carboxypeptidases/*isolation & purification/metabolism ; cell membrane/enzymology ; centrifugation, density gradient ; chromatography, affinity ; chromatography, deae-cellulose ; electrophoresis, paper ; escherichia coli/cytology/*enzymology ; glycine ; hydrogen-ion concentration ; kinetics ; microscopy, electron ; mutation ; osmolar concentration ; peptidoglycan/biosynthesis ; solubility ; spectrophotometry ; spectrophotometry, ultraviolet ; surface-active agents
[en] A transpeptidase activity in Escherichia coli was measured independently of other enzymes involved in peptidoglycan synthesis by quantitating the formation of UDP-N-acetylmuramyl-l-alanyl-y-d-glutamyl-(l)-meso-diaminopimelyl-(l)-d-alanyl-[14C]glycine when UDP-N-acetylmuramyl-l-alanyl-y-d-glutamyl-(l)-meso-diaminopimelyl-(l-d-alanyl-d-alanine was used as donor substrate and [14C]glycine as acceptor in a transfer reaction. After extraction of membrane envelopes with Brij-36T and subsequent ammonium sulfate precipitation, DEAE-cellulose chromatography revealed two major fractions; one not adsorbed to the ion-exchange resin and the other adsorbed. The fraction which was bound to DEAE-cellulose was bound to and could be eluted from an ampicillin affinity chromatography system while the fraction not bound to DEAE-cellulose was also not bound to the ampicillin column. Both unbound and bound ampicillin fractions exhibited dd-carboxypeptidase and transpeptidase activities although for equivalent dd-carboxypeptidase activity, the bound ampicillin fraction required about five times more glycine acceptor to achieve the same amount of transpeptidation as the unbound ampicillin fraction.
Fonds de la Recherche Fondamentale Collective
Researchers ; Professionals
http://hdl.handle.net/2268/83100
10.1111/j.1432-1033.1974.tb03285.x

File(s) associated to this reference

Fulltext file(s):

FileCommentaryVersionSizeAccess
Restricted access
POLLOCK_1974_fractionation.pdfPublisher postprint4.05 MBRequest copy

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.