Chemically phosphorylated protamine: A new substrate for the study of phosphoprotein phosphatase activity

Buddy Ullman, Robert L. Perlman

Research output: Contribution to journalArticle

23 Scopus citations

Abstract

A method for the chemical phosphorylation of seryl residues in protamine has been developed. Both non-radioactive and [33P]phosphoprotamine have been prepared and characterized. Phosphoprotein phosphatases from a variety of mammalian tissues release inorganic phosphate from phosphoprotamine. Chemically phosphorylated protamine is a useful new substrate for the study of these phosphoprotein phosphatases.

Original languageEnglish (US)
Pages (from-to)424-431
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume63
Issue number2
DOIs
StatePublished - Mar 17 1975

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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