Resolution of adenylate cyclase sensitive and insensitive to Ca2+ and calcium-dependent regulatory protein (CDR) by CDR-Sepharose affinity chromatography

K. R. Westcott, D. C. La Porte, D. R. Storm

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115 Scopus citations

Abstract

Partially purified adenylate cyclase [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1] from bovine brain cortex was fractionated into two separate forms by calcium-dependent regulatory protein (CDR)-Sepharose affinity chromatography. The major form of the enzyme, comprising ~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. This study directly demonstrates that brain cortex contains Ca2+.CDR-sensitive and -insensitive forms of adenylate cyclase and indicates that 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.

Original languageEnglish (US)
Pages (from-to)204-208
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume76
Issue number1
DOIs
StatePublished - 1979

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