title: Hair acid phosphatase: multiple forms, glycoprotein nature and characterization.
abstract: Multiple forms of guinea pig hair acid phosphatase and glycoprotein types have been studied by isoelectric focusing and concanavalin-A-Sepharose chromatography. The enzyme appeared under many different forms using electrophoresis. They had similar properties (optimum pH, inhibition studies). The bulk of hair acid phosphatase was bound to concanavalin-A-Sepharose, and approximately 60% of the activity was eluted with alpha-methyl-D-glucoside. This finding strongly indicates that hair phosphatase is a glycoprotein. The enzyme was partially purified by a procedure including DEAE-cellulose and CM-cellulose chromatography, and gel filtration on Sephadex G-100. The enzyme showed similar properties to those of lysosomal acid phosphatase from other organs.
mesh_terms: D000135:Acid Phosphatase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002846:Chromatography, Affinity; D006168:Guinea Pigs; D006197:Hair / Q000201:enzymology*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008297:Male; D008757:Methylglucosides; D013379:Substrate Specificity
chemical_list: D008757:Methylglucosides; C027020:methylglucoside; D000135:Acid Phosphatase