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Phosphorylation of protein components of isolated zymogen granule membranes from the rat pancreas

par Lambert, Monique;Camus, Jean Claude ;Christophe, Jean
Référence FEBS letters, 49, 2, page (228-232)
Publication Publié, 1974

Article révisé par les pairs

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Résumé :

Some properties were examined of the isolated membranes of zymogen granules from the rat pancreas. It was possible to detect an endogenous protein kinase activity capable of phosphorylating 8 to 10 membrane protein constituents as well as added histones. Cyclic adenosine monophosphate (AMP), and cyclic guanosine monophosphate (GMP), to a lesser extent, exerted moderate stimulatory effects. These effects of cyclic nucleotides on membrane phosphorylation became more apparent upon addition of a partially purified soluble protein kinase also extracted from the rat pancreas.