Evidence for two distinct adenylate cyclase catalysts in rat brain

FEBS Letters
F CoussenJ C Cavadore

Abstract

The Lubrol-soluble adenylate cyclase activity of brain synaptosomal membranes appeared, upon gel filtration or sucrose gradient centrifugation, as two overlapping peaks. Fractions corresponding to the peak of the largest Stokes radius (Biogel pool 1) or highest s value (gradient pool 1) contained an adenylate cyclase activity which could be detected whatever the enzyme assay conditions. In contrast, in fractions from the second peak (Biogel pool 2 or gradient pool 2), forskolin was needed to reveal adenylate cyclase activity. The enzyme activity of each Biogel pool was retained by forskolin-agarose and eluted by forskolin with a 34-83% yield. A polypeptide of 155 kDa made up 80% of the forskolin-agarose eluate 1, whereas it was almost absent from eluate 2. Since data from various groups point to the 155 kDa polypeptide as a brain adenylate cyclase catalyst, still another distinct catalyst of lower molecular mass is likely to be present in brain.

References

Jan 1, 1975·Proceedings of the National Academy of Sciences of the United States of America·C O BrostromD J Wolff
Jan 26, 1976·Biochemical and Biophysical Research Communications·T J LynchW Y Cheung
Oct 1, 1985·Proceedings of the National Academy of Sciences of the United States of America·F CoussenA Monneron
May 1, 1985·Proceedings of the National Academy of Sciences of the United States of America·E PfeufferT Pfeuffer
Sep 1, 1985·Proceedings of the National Academy of Sciences of the United States of America·M S Livingstone
Dec 1, 1973·Analytical Biochemistry·W Schaffner, C Weissmann
Jan 1, 1984·Methods in Enzymology·C R MerrilM L Van Keuren

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