Evidence for a dissociable protein subunit required for calmodulin stimulation of brain adenylate cyclase.
- 1 November 1979
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 76 (11), 5582-5586
- https://doi.org/10.1073/pnas.76.11.5582
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+ .cntdot. calmodulin was 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+ .cntdot. calmodulin activation required the presence of 5''-guanylyl imidodiphosphate. The factor required for restoration of Ca2+ .cntdot. calmodulin stimulation was sensitive to heat, trypsin digestion and N-ethylmaleimide. This adenylate cyclase activity probably requires the presence of 1 or more guanyl nucleotide binding subunits for calmodulin sensitivity.This publication has 27 references indexed in Scilit:
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