Properties of low-molecular-weight acid phosphatases isolated from cytosol and chromatin of rat liver.
1. Acid phosphatases (orthophosphoric-monoester phosphohydrolases, acid optimum, EC 3.1.3.2) of low molecular weight were isolated from cytosol and chromatin of rat liver cells. The cytosolic enzyme was homogeneous on SDS-polyacrylamide-gel electrophoresis at pH 8.3 (mol. wt. 16 000+/-3000). Both enzymes showed similar electrophoretic mobility and molecular weight but they differed in substrate specificity, response to inhibitors and susceptibility to SH-protecting reagents.
D000135:Acid Phosphatase / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002843:Chromatin / Q000201:enzymology*; D003600:Cytosol / Q000201:enzymology; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight; D051381:Rats; D013379:Substrate Specificity; D013439:Sulfhydryl Reagents / Q000494:pharmacology
D002843:Chromatin; D013439:Sulfhydryl Reagents; D000135:Acid Phosphatase