1.
Biochem Biophys Res Commun
; 67(1): 139-48, 1975 Nov 03.
Article
in English
| MEDLINE
| ID: mdl-1106406
Subject(s)
Bacterial Proteins/isolation & purification , Carboxypeptidases/antagonists & inhibitors , Escherichia coli/enzymology , Alanine , Bacterial Proteins/pharmacology , Cations, Divalent , Cations, Monovalent , Chlorides/pharmacology , Drug Stability , Escherichia coli/analysis , Escherichia coli/growth & development , Kinetics , Potassium/pharmacology , Sodium/pharmacology
2.
Purification of D-alanine carboxypeptidase from Escherichia coli B on a penicillin-Sepharose column.
Biochem J
; 147(1): 131-7, 1975 Apr.
Article
in English
| MEDLINE
| ID: mdl-1098657
ABSTRACT
1. A soluble D-alanine carboxypeptidase from Escherichia coli strain B was purified on a p-aminobenzylpenicillin-Sepharose column. This one-step chromatography followed by an (NH4)2SO4 precipitation yielded an enzyme purified 1200-fold and some of its properties are reported. 2. The pure D-alanine carboxypeptidase was devoid of D-alanine carboxypeptidase II activity and migrated as a single protein band on analytical disc gel electrophoresis. 3. Triton X-100 in the purification procedure is an absolute requirement for obtaining a stable enzyme. 4. The enzymic activity of D-alanine carboxypeptidase was greatly affected in solution of high salt concentrations and varied somewhat with the nature of the cation tested.
Subject(s)
Carboxypeptidases/isolation & purification , Escherichia coli/enzymology , Alanine , Ampicillin , Chemical Precipitation , Chromatography, Affinity , Electrophoresis, Disc , Polyethylene Glycols , Sepharose , Sodium Chloride
3.
Methods Enzymol
; 34: 398-401, 1974.
Article
in English
| MEDLINE
| ID: mdl-4615244
4.
Arch Biochem Biophys
; 136(2): 325-30, 1970 Feb.
Article
in English
| MEDLINE
| ID: mdl-5461614