Resolution of adenylate cyclase sensitive and insensitive to Ca2+ and calcium-dependent regulatory protein (CDR) by CDR-sepharose affinity chromatography.
- 1 January 1979
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 76 (1) , 204-208
- https://doi.org/10.1073/pnas.76.1.204
Abstract
Partially purified adenylate cyclase [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1] from bovine brain cortex was fractionated into 2 separate forms by Ca-dependent regulatory protein (CDR) Sepharose affinity chromatography. The major form of the enzyme, comprising .apprxeq. 80% of the applied activity, did not bind to the affinity column in the presence of Ca2+ and was insensitive to the CDR. Approximately 20% of adenylate cyclase activity was absorbed to CDR-Sepharose in the presence of Ca2+. This activity was stimulated by Ca2+ and CDR. Brain cortex contains Ca2+ .cntdot. CDR-sensitive and -insensitive forms of adenylate cyclase. CDR-Sepharose may be a useful tool for purification of adenylate cyclase. The Ca2+-stimulated adenylate cyclase was purified at least 55-fold with a 13% yield.This publication has 30 references indexed in Scilit:
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