Demonstration of separate phosphotyrosyl- and phosphoseryl-histone phosphatase activities in the plasma membranes of a human astrocytoma

Jose F. Leis, Aileen F. Knowles, Nathan O. Kaplan

Research output: Contribution to journalArticle

14 Scopus citations

Abstract

A plasma membrane preparation from a human astrocytoma contained p-nitrophenyl phosphate (pNPP), phosphotyrosyl histone, and phosphoseryl histone hydrolysis activities. The pNPPase and phosphotyrosyl histone phosphatase activities were inhibited by vanadate, whereas the phosphoseryl histone phosphatase activity was not; the latter activity was inhibited by pyrophosphate and nucleoside di- and triphosphates. When the membranes were solubilized by Triton X-100 and the solubilized proteins were subjected to column chromatography on DEAE-Sephadex, Sepharose 6B-C1, and wheat germ agglutinin-Sepharose 4B columns, the pNPPase activity coeluted with the phosphotyrosyl histone phosphatase activity, and was separable from the phosphoseryl histone phosphatase activity. The results from column chromatography also indicated that there may be multiple phosphotyrosyl and phosphoseryl protein phosphatases in the plasma membranes.

Original languageEnglish (US)
Pages (from-to)320-326
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume239
Issue number2
DOIs
StatePublished - Jun 1985

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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