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pubmed-article:2494070pubmed:abstractTextAdrenal medullary homogenates and chromaffin granule membranes were separated by SDS-polyacrylamide gel electrophoresis and GTP-binding proteins detected using [alpha-32P]GTP binding to nitrocellulose blots. Four GTP-binding polypeptides of 24, 22, 20 and 18 kDa were routinely found in medullary homogenates and all were also found in isolated chromaffin granule membranes. The GTP-binding polypeptides co-sedimented with granule membrane markers following separation on sucrose gradients. On the basis of trypsin sensitivity and resistance to extraction, the GTP-binding proteins appeared to be tightly bound to the cytoplasmic surface of the granules. One or more of the secretory granule GTP-binding proteins could be involved in exocytosis in adrenal chromaffin cells.lld:pubmed
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pubmed-article:2494070pubmed:articleTitleLow molecular mass GTP-binding proteins of adrenal chromaffin cells are present on the secretory granule.lld:pubmed
pubmed-article:2494070pubmed:affiliationDepartment of Physiology, University of Liverpool, England.lld:pubmed
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