Resolution of the low-molecular-weight acid phosphatase in avian pectoral muscle into two distinct enzyme forms.
Three distinct acid phosphatases were recently reported in avian breast muscle [J. H. Baxter and C. H. Suelter (1984) Arch. Biochem. Biophys. 228, 397-406]. Of the increased acid phosphatase activity in dystrophic muscle compared to normal muscle, 84% can be accounted for as a low-molecular-weight, cytosolic form. This low-molecular-weight form has now been purified and resolved into two distinct forms, A and B, differing in isoelectric point, apparent molecular weight, substrate specificity, and activation by guanosine. One of the two enzymes exhibits substrate inhibition with 4-methylumbelliferyl phosphate, indicating a further difference. The evidence suggests that both enzymes are Class IV acid phosphatases. Their concentrations are highest in tissues with a high catabolic activity.
D000135:Acid Phosphatase / Q000302:isolation & purification*; D000818:Animals; D002645:Chickens; D004789:Enzyme Activation / Q000187:drug effects; D006151:Guanosine / Q000494:pharmacology; D007525:Isoelectric Focusing; D007700:Kinetics; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D009137:Muscular Dystrophy, Animal / Q000201:enzymology; D013379:Substrate Specificity; D014018:Tissue Distribution
D006151:Guanosine; D000135:Acid Phosphatase