The intracellular localization of glycolate oxidoreductase in Escherichia coli.
Distribution of glycolate oxidoreductase in cell-free extracts of E. coli grown in mineral medium containing sodium glycolate has been studied. The enzyme was found to be largely associated with the cytoplasmic membranes. Homologous antiserum to the membranes inhibited the enzyme activity completely after the solubilization of the intact membranes with Triton X-100. Results on the effect of pronase on glycolate oxidoreductase activity confirmed that part of the enzyme is exposed to the surface of the membrane.
Sallal
A K
AK
Department of Botany and Microbiology, Faculty of Science, University of Kuwait.
Nimer
N A
NA
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D002458:Cell Fractionation; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D013347:Subcellular Fractions / Q000201:enzymology; D014461:Ultracentrifugation
D000429:Alcohol Oxidoreductases; C020821:glycollate oxidase