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.