Evidence of a dissociable protein subunit required for calmodulin stimulation of brain adenylate cyclase

W. A. Toscano, K. R. Westcott, D. C. LaPorte, D. R. Storm

Research output: Contribution to journalArticlepeer-review

34 Scopus citations

Abstract

An adenylate cyclase [ATP pyrophosphate lyase (cyclizing), EC 4.6.1.1] preparation that is not stimulated by NaF,5'-guanylyl imidodiphosphate, or Ca2+-calmodulin has been isolated from bovine cerebral cortex by Affi-Gel Blue chromatography and calmodulin-Sepharose chromatography. Sensitivity to these effectors was restored by incubation of the adenylate cyclase preparation with detergent-solubilized protein from bovine cerebral cortex. Reconstitution of Ca2+ calmodulin activation required the presence of 5'-guanylyl imidodiphosphate. The factor required for restoration of Ca2+ calmodulin stimulation was sensitive to heat, trypsin digestion, and N-ethylmaleimide. These observations suggested that this adenylate cyclase activity requires the presence of one or more guanyl nucleotide binding subunits for calmodulin sensitivity.

Original languageEnglish (US)
Pages (from-to)5582-5586
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume76
Issue number11
DOIs
StatePublished - 1979

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