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Evidence for two distinct adenylate cyclase catalysts in rat brain
Author(s) -
Coussen Francoise,
Guermah Mohamed,
d'Alayer Jacques,
Monneron Ariane,
Haiech Jacques,
Cavadore Jean-Claude
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80983-8
Subject(s) - cyclase , adenylate kinase , forskolin , chemistry , biochemistry , stokes radius , agarose , enzyme , size exclusion chromatography , chromatography , in vitro
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.