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A Repressible Alkaline Phosphatase in Neurospora crassa

II. ISOLATION AND CHEMICAL PROPERTIES

From the ¹ From the Department of Biological Chemistry, UCLA School of Medicine, Los Angeles, California 90024

The repressible alkaline phosphatase in a wild type strain of Neurospora crassa was purified to apparent homogeneity, as ascertained from centrifugal and electrophoretic data, and was characterized by physical and chemical methods. The native protein molecule has a molecular weight of 154,000, as determined by the method of sedimentation equilibrium. This species can be dissociated in the presence of 6 m guanidine-mercaptoethanol into subunits possessing a molecular weight of 77,000. Determinations of the amino acid and sugar composition of this enzyme disclosed that it is a glycoprotein in which the carbohydrates constitute about 11.5% of the total weight. In derepressed cultures of the mold, this enzyme represents about 1% of the total protein.

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