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- W1979032148 abstract "Reversible methylation is a post-translocational modification of proteins that plays an important role in regulatory processes in both prokaryotes and eukaryotes [ 1,2]. The free carboxyl groups of methyl acceptor proteins (MAPS) can be esterified by methyl groups derived from Sadenosyhnethionine (SAM) in a reaction catalysed by protein carboxymethylase @CM). 3-isobutyl-1-methylxanthine (IBMX) and bovine albumin were from Sigma (London) Chemical Co. (Poole, Dorset). S-Adenosyl-L[methyl-‘Hlmethionine (72 Ci/mmol) and L-[methyZ-3H]methionine (93 Ci/ mmol) were from the Radiochemical Centre (Amersham, Bucks). Other reagents, of the purest grade available, were from British Drug Houses Chemicals (Poole, Dorset). Calmodulin, prepared from bovine brain, was a gift from Dr M. P. Esnouf of this department. In eukaryotes, protein carboxymethylation has been implicated in sperm mobility [3], leucocyte chemotaxis [4] and neural function [5]. Several studies have also suggested that protein carboxymethylation may be involved in stimulus-secretion coupling. Secretory tissues for which support for this hypothesis has been obtained include adrenal medulla [6], parotid [3] and exocrine pancreas [7] (but see also [S]). In addition it has been shown that calmodulin is a notably good substrate for PCM and that methylation of calmodulin diminishes its ability to activate cyclic nucleotide phosphodiesterase [9]. Since there is a growing body of evidence to implicate calmodulin in Ca2+-dependent stimulus-secretion coupling [lo121, PCM could also be linked to secretion via calmodulin methylation. 2.2. Isolation of islets Islets of Langerhans were isolated from pancreases of fed male Wistar rats by a collagenase method [13]." @default.
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- W1979032148 date "1982-02-08" @default.
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- W1979032148 title "Protein carboxymethylation in rat islets of Langerhans" @default.
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- W1979032148 doi "https://doi.org/10.1016/0014-5793(82)80397-9" @default.
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