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Phosphorylation of protein components of isolated zymogen granule membranes from the rat pancreas
Author(s) -
Lambert Monique,
Camus Jean,
Christophe Jean
Publication year - 1974
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(74)80518-1
Subject(s) - boulevard , medical school , library science , chemistry , medicine , computer science , engineering , medical education , civil engineering
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.SCOPUS: ar.jinfo:eu-repo/semantics/publishe