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.