Linked Life Data

9877327

Source:http://linkedlifedata.com/resource/pubmed/id/9877327

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pubmed-article:9877327pubmed:abstractTextBeta-adrenergic or cholinergic stimulation of the rat parotid gland was earlier shown to induce dephosphorylation of endogenous destrin- and cofilin-like proteins, which are phosphorylated in resting cells at Ser residues probably present near the N-terminals. The primary structures and phosphorylation sites were determined here. The rat destrin-like protein had a sequence 95% identical to the cDNA-derived sequence of porcine destrin. The rat cofilin-like protein was 98% identical to that of porcine cofilin. Each protein lacked the initiator Met and began with an acetylalanine residue followed by a Ser residue. The N-terminal peptides generated with endoproteinase Asp-N were isolated; they were each phosphorylated at Ser-2. Earlier work had shown that partial cleavage of the phosphorylated destrin- and cofilin-like proteins with cyanogen bromide provides unphosphorylated 16.7- and 18.3-kDa fragments, respectively. It was here confirmed that they contained all the Ser residues other than those present in the N-terminal peptides. From these observations, it was now concluded that the destrin- and cofilin-like proteins are rat parotid destrin and cofilin (non-muscle type), respectively, and that each protein is phosphorylated exclusively at Ser-2 in resting cells and dephosphorylated at this site in response to beta-adrenergic or cholinergic stimulation.lld:pubmed
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pubmed-article:9877327pubmed:dateRevised2008-11-21lld:pubmed
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pubmed-article:9877327pubmed:articleTitleComplete amino acid sequences and phosphorylation sites, determined by Edman degradation and mass spectrometry, of rat parotid destrin- and cofilin-like proteins.lld:pubmed
pubmed-article:9877327pubmed:affiliationDepartment of Biochemistry, School of Dentistry, Aichi-Gakuin University, Nagoya, Japan.lld:pubmed
pubmed-article:9877327pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9877327pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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