Fundamental biochemical and immunological aspects of prostatic acid phosphatase

M. F. Lin, C. L. Lee, J. W. Wojcieszyn, M. C. Wang, L. A. Valenzuela, G. P. Murphy, T. M. Chu

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


Prostatic acid phosphatase (PAP) was purified from human malignant prostate tissue by means of ammonium sulfate fractionation followed by sequential chromatographies of ion exchange, affinity column, and gel filtration. PAP has a molecular weight of 100,000 and consists of two subunits of 50,000. Owing, in part, to sialic acid contents in the molecule, PAP has multiple isoelectric points (pIs) at 4.2‐5.5. In 0.2 M citrate, PAP has the highest affinity (Km 9.2 × 10−5 M) in hydrolyzing α‐naphthyl phosphate among the phosphomonoesters. Tartrate and heat at 37†C for 2 hours almost completely inhibit PAP enzymic activity. By immunoprecipitate technique, anti‐PAP heteroantiserum exhibited a distinct immunologic characteristics. Further, PAP possessed different antibody‐binding site from enzyme hydrolytic site.

Original languageEnglish (US)
Pages (from-to)415-425
Number of pages11
JournalThe Prostate
Issue number4
StatePublished - 1980
Externally publishedYes


  • characterization
  • isolation
  • prostatic acid phosphatase

ASJC Scopus subject areas

  • Oncology
  • Urology


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