Monoclonal antibody specific to acid phosphatase isoenzyme 4

Howard Dang, Kwok‐Wai ‐W Lam, Chin‐Yang ‐Y Li, Lester E. Wold, Tsieh Sun, Lung T. Yam

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

Prostatic acid phosphatase isoenzyme 4 was purified by ion exchange column chromatography, followed by high pressure liquid chromatography. The highly purified enzyme was used to produce monoclonal antibody from immunized BALB/c mice. The antibody was specific to isoenzyme 4, with negligible affinity to isoenzyme 2. The specificity of the monoclonal antibody was evaluated by Western blot analysis and by inhibition of radioimmunoassay. Immunohistochemistry method using the antibody to isoenzyme 2 showed heavy staining on the cell surface in contrast to the even staining throughout the cytoplasm when monoclonal anti‐isoenzyme 4 was used. These results reflect the secretory nature of isoenzyme 2 and the non‐secretory nature of isoenzyme 4.

Original languageEnglish (US)
Pages (from-to)47-55
Number of pages9
JournalThe Prostate
Volume9
Issue number1
DOIs
StatePublished - 1986

Keywords

  • electrophoresis
  • immunohistochemistry
  • radioimmunoassay

ASJC Scopus subject areas

  • Oncology
  • Urology

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