Purification And Characterization Of Human Prostatic Acid Phosphatase

B. K. Choe, E. J. Pontes, I. McDonald, N. R. Rose

Research output: Contribution to journalArticlepeer-review

Abstract

Human prostatic acid phosphatase (orthophosphoric monoester phospho-hydrase, EC 3.1.3.2) is purified to homogeneity by standard procedures which include CM-Sephadex, Con A affinity chromatography and gel filtration. The purified enzyme is antigenically specific and has a M.W. of 100,000 with subunit M.W. of 48,000. However, the enzyme exhibited charge heterogeneity. Two major electrophoretic or chromatographic isozymic forms of PAP were separated by DEAE-Sephadex chromatography and their immunochemical identity was studied by immunodiffusion before and after the neuraminidase digestion. Quantitative precipitin and inhibition experiments showed immunological identity of the two chromatographic iso-zymes. Immunologic specificity of this enzyme resides on the protein moiety rather than the carbohydrate residue, although the latter group is mostly responsible for the charge group heterogeneity of the enzyme.

Original languageEnglish (US)
Pages (from-to)73-89
Number of pages17
JournalPreparative Biochemistry
Volume8
Issue number1
DOIs
StatePublished - Jan 1 1978

ASJC Scopus subject areas

  • Biochemistry
  • Genetics

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