Abstract
Liver post-mitochondrial supernatant from diabetic rats showed a decrease in the [ 3H] cAMP binding activity which was associated with a decrease in the number of cAMP binding sites. On the other hand, the cAMP binding activity of nuclear fractions from diabetic rat liver was not significantly different than that of control. The cAMP binding activity of post-mitochondrial supernatant was further analyzed by using 8-azido-[ 32P] cAMP, a photoaffinity probe for cAMP binding sites. The diabetic supernatants showed a selective reduction in the photolabeling of a protein band representing the regulatory subunit of type I cAMP-dependent protein kinase without any appreciable change in the photolabeling of regulatory subunit of type II cAMP-dependent protein kinase.
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More From: Biochemical and Biophysical Research Communications
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