Specificity of a phosphatase for phospholipid, Ca2+-dependent protein kinase-phosphorylated histone H1 resides in the catalytic subunit

Harry LeVine, Naji Sahyoun, Randy McConnell, Duane Bronson, Pedro Cuatrecasas

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

A protein phosphatase from liver which acts preferentially on histone phosphorylated with phospholipid, Ca2+-dependent protein kinase has been purified and the intrinsic specificity determined to reside in the catalytic subunit of the enzyme complex. Comparison with a preparation of pork heart protein phosphatase suggests that this specificity may be a general property of a class of protein phosphatases. Protein kinase C-phosphorylated histone H1 represents an improved substrate for phosphatase detection providing a five to tenfold greater sensitivity than other substrates including cAMP-dependent protein kinase phosphorylated H1.

Original languageEnglish
Pages (from-to)278-283
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume118
Issue number1
DOIs
StatePublished - Jan 13 1984

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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