Isolation and chemical properties of a repressible acid phosphatase in Neurospora crassa.

Abstract 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.

• Publication year

  1971

• Venue

  Journal of Biological Chemistry

• Publication date

  1971-03-10

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/s0021-9258(19)76988-9PMID 5545084
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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