Acylphosphatase from human skeletal muscle: purification, some properties and levels in normal and myopathic muscles.
Human skeletal muscle acylphosphatase was purified by immunoaffinity chromatography using anti-horse muscle acylphosphatase antibodies. The three forms of the enzyme present in human muscle are very similar to those found in muscles of other animal species. The two main forms, Hu 1 and Hu 3, were also characterized with respect to molecular weight and some kinetic properties. Levels of acylphosphatase activity were measured in specimens of muscle from normals and from patients with various forms of muscular dystrophies and other myopathies. Acylphosphatase activity appears to be lower in all myopathic forms considered than in controls, and seems to be correlated with percentage of Ca2+ activation of (Ca2+ + Mg2+)-ATPase.
D017766:Acid Anhydride Hydrolases; D000596:Amino Acids / Q000032:analysis; D017301:Ca(2+) Mg(2+)-ATPase / Q000032:analysis; D000252:Calcium-Transporting ATPases / Q000032:analysis; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007120:Immunochemistry; D009132:Muscles / Q000201:enzymology*; D009135:Muscular Diseases / Q000201:enzymology*; D010744:Phosphoric Monoester Hydrolases / Q000302:isolation & purification*; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D000596:Amino Acids; D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases; D010744:Phosphoric Monoester Hydrolases; D000097024:Acylphosphatase