Isolation and Chemical Properties of a Repressible Acid Phosphatase in Neurospora crassa

An orthophosphate-repressible acid phosphatase from a wild type strain of Neurospora crassa was purified to apparent homogeneity. The degree of purity was ascertained on the basis of chromatographic, electrophoretic, and centrifugal data. Sedimentation equilibrium analyses indicated the native molecule has a molecular weight of about 85,000 and can be dissociated in the presence of 6 m guanidine-mercaptoethanol into 2 physically indistinguishable subunits. The amino acid and sugar composition is reported for the enzyme, a glycoprotein in which mannose and glucosamine residues account for 9.5% of the molecular weight.