Activation of pigeon erythrocyte adenylate cyclase by cholera toxin partial purification of an essential macromolecular factor from horse erythrocyte cytosol

Harry Le Vine, Pedro Cuatrecasas

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

A cytosolic, macromolecular factor required for the cholera toxin-dependent activation of pigeon erythrocyte adenylate cyclase and cholera toxin-dependent ADP-ribosylation of a membrane-bound 43 000 dalton polypeptide has been purified 1100-fold from horse erythrocyte cytosol using organic solvent precipitation and heat treatment. This factor, 13 000 daltons, does not absorb to anionic or cationic exchange resins, is sensitive to trypsin or 10% trichloroacetic acid and is not extractable by diethyl ether. Activation of adenylate cyclase by cholera toxin requires the simultaneous presence of ATP (including possible trace GTP), NAD+, dithiothreitol, cholera toxin, membranes and the cytosolic macromolecular factor. Reversal of cholera toxin activation of adenylate cyclase, and of the toxin-dependent ADP-ribosylation, requires the presence of the cytosolic factor. The ability of the purified cytosolic factor to influence the hormonal sensitivity of liver membrane adenylate cyclase may provide clues to its physiological functions.

Original languageEnglish
Pages (from-to)248-261
Number of pages14
JournalBiochimica et Biophysica Acta - General Subjects
Volume672
Issue number3
DOIs
StatePublished - Feb 5 1981

Keywords

  • (Erythrocyte)
  • Adenylate cyclase activation
  • Cholera toxin
  • Macromolecular factor

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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