Changes in allosteric properties of phosphofructokinase bound to erythrocyte membranes

N. S. Karadsheh, K. Uyeda

Research output: Contribution to journalArticle

69 Scopus citations

Abstract

Human and rabbit erythrocyte membranes prepared by hypotonic hemolysis contained 5 to 15% of the phosphofructokinase in the erythrocytes. The membrane bound phosphofructokinase can be eluted by a saline wash. Human erythrocyte and rabbit muscle phosphofructokinase bind to the saline-washed membranes. This binding is specific for the inner surface of the membrane. The amount of phosphofructokinase bound is dependent on pH; at pH 7, 6 times more enzyme is bound than at pH 7.5. Unlike free phosphofructokinase, the membrane bound phosphofructokinase is not inhibited by ATP or 2,3 diphosphoglycerate and its fructose 6 P saturation curve is nonsigmoidal.

Original languageEnglish (US)
Pages (from-to)7418-7420
Number of pages3
JournalJournal of Biological Chemistry
Volume252
Issue number21
StatePublished - Dec 1 1977

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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