title: Multiple acid phosphatases in avian pectoral muscle--the postmicrosomal supernatant acid phosphatase is elevated in avian dystrophic muscle.
abstract: There are at least three forms of acid phosphatase in avian pectoralis muscle differing in molecular weight, subcellular location, and response to various substrates and inhibitors. These enzymes are separated by differential sedimentation into postmicrosomal supernatant, lysosomal, and microsomal activities with apparent molecular weights in Triton X-100 of 68,000, 198,000, and 365,000, respectively. All of the enzymes show acid pH optima (pH approximately 5), but the postmicrosomal supernatant form is distinctly different from the other two forms in its resistance to most common phosphatase inhibitors and in its reduced activity against several organic phosphates. Quantitation of these three forms of acid phosphatase in normal and dystrophic avian pectoralis muscle shows that the postmicrosomal supernatant form is significantly elevated in dystrophic muscle; at 33 days ex ovo, 84% of the increased acid phosphatase activity in dystrophic muscle can be attributed to the postmicrosomal supernatant form. The microsomal form is only slightly elevated; the level of the lysosomal form is not altered.
mesh_terms: D000135:Acid Phosphatase / Q000378:metabolism*; D000818:Animals; D002645:Chickens; D002850:Chromatography, Gel; D003600:Cytosol / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D008247:Lysosomes / Q000201:enzymology; D008861:Microsomes / Q000201:enzymology; D009132:Muscles / Q000201:enzymology*; D009137:Muscular Dystrophy, Animal / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D000135:Acid Phosphatase