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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 approximately 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.
K R Westcott, and
D C La Porte, and
D R Storm
May 1977,
Archives of biochemistry and biophysics,
K R Westcott, and
D C La Porte, and
D R Storm
January 1985,
Comparative biochemistry and physiology. B, Comparative biochemistry,
K R Westcott, and
D C La Porte, and
D R Storm
March 1979,
FEBS letters,
K R Westcott, and
D C La Porte, and
D R Storm
January 1987,
Infection and immunity,
K R Westcott, and
D C La Porte, and
D R Storm
December 1981,
Archives of biochemistry and biophysics,
K R Westcott, and
D C La Porte, and
D R Storm
February 1979,
Biochemical and biophysical research communications,
K R Westcott, and
D C La Porte, and
D R Storm
May 1986,
Calcified tissue international,
K R Westcott, and
D C La Porte, and
D R Storm
December 1981,
The Journal of biological chemistry,
K R Westcott, and
D C La Porte, and
D R Storm
January 1980,
Annals of the New York Academy of Sciences,
K R Westcott, and
D C La Porte, and
D R Storm
November 1984,
Archives of biochemistry and biophysics,
