Human prostatic acid phosphatases: I. isolation

B. K. Choe, E. J. Pontes, S. Bloink, N. R. Rose

Research output: Contribution to journalArticlepeer-review

Abstract

A new purification procedure is described for the human prostatic acid phosphatase. The procedure included carboxy-methyl-Sephadex and Concanavalin A affinity column chromatography. The purified enzyme has a high specific enzyme activity and is free from any extraneous proteins judging from immunochemical criteria and biochemical criteria such as SDS-polyacrylamide gel electrophoresis. The purified enzyme produced a monospecific anti-PAP antisera in animals and this anti-PAP antibody did not cross-react with other human acid phosphatases.

Original languageEnglish (US)
Pages (from-to)221-226
Number of pages6
JournalSystems Biology in Reproductive Medicine
Volume1
Issue number3
DOIs
StatePublished - Jan 1 1978

ASJC Scopus subject areas

  • Reproductive Medicine
  • Urology

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