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- W2038584459 abstract "The localization of guanylate cyclase in bovine adrenal medulla was explored by preparation of subcellular organelles. Forty per cent of the activity was recovered in the soluble fraction (cytosol), and 46% in the low-speed (800g) pellet as particulate. In order to determine the exact localization of the particulate enzyme, continuous sucrose density gradient centrifugation was used. The results indicate that guanylate cyclase activity sedimented together with acetylcholinesterase and adenylate cyclase, two plasma membrane markers. Enrichment of specific activity over that present in the crude chromaffin granule fraction was identical for these three enzymes (from 4.4 to 6.2-fold). Particulate guanylate cyclase appears therefore to be a constituent of plasma membranes. The non-ionic detergent Triton X-100 and the natural phospholipid, lysolecithin, stimulated particulate guanylate cyclase activity 20-fold, but that of the soluble enzyme only 2- to 3-fold. The kinetic behaviour of particulate guanylate cyclase was not altered by treatment with lysolecithin: the Hill n coefficient for guanosine 5′-triphosphate remained close to 1.35 and the S0.5 value to 320 μM. Among lecithin, lysophosphatidyl ethanolamine and phosphatidyl serine, lysolecithin was the only phospholipid to induce activation of particulate guanylate cyclase. Incubation of membranes with phospholipase A2 led to a 5-fold stimulation of particulate guanylate cyclase activity, while the soluble enzyme activity was not affected. These results suggest a possible role for lysolecithin in the regulation of the intracellular levels of cyclic guanosine monophosphate during or following the excitation-secretion coupling process in the medullary cell." @default.
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- W2038584459 date "1978-01-01" @default.
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- W2038584459 title "Guanylate cyclase from bovine adrenal medulla: Subcellular distribution and studies on the effect of lysolecithin on enzyme activity" @default.
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