Regulation of rat placental phosphorylase

Elliott Ross, Donal Walsh

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Abstract

Glycogen phosphorylase (α-1,4-glucan: orthophosphate glucosyltransferase, EC 2.4.1.1) from rat placenta has been shown to exist in AMP-dependent and -independent forms that are designated phosphorylase b and a, respectively. Phosphorylase b exhibits a Ka of 1.5·10-4 M for AMP and is stimulated by 0.7 M Na2SO4 in the presence or absence of the nucleotide; in contrast, phosphorylase a is inhibited by Na2SO4. Placental extracts contain a phosphorylase kinase, a phosphorylase phosphatase and a cyclic AMP-dependent protein kinase which are presumed to be associated with the control of glycogenolysis in this tissue.

Original languageEnglish (US)
Pages (from-to)490-496
Number of pages7
JournalBBA - General Subjects
Volume264
Issue number3
DOIs
StatePublished - May 16 1972

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ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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