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- W1609365613 abstract "Abstract Adenyl cyclase activity of the parotid gland dropped by about 50% after intensive secretion of digestive enzymes produced by isoprenaline injection. No adenyl cyclase was detected in parotid saliva obtained by cannulation of the duct. The proteins which were secreted represented half of the total protein in the gland. Fractionation of the gland homogenate showed that the largest proportion of adenyl cyclase activity was located in the 200 x g fraction, probably in cell membranes. There was no significant activity in the zymogen granules although these structures play a key role in the secretion process induced via cyclic adenosine 3',5'-monophosphate. Various preparations of rat parotid adenyl cyclase and their properties are described. The insoluble membrane-bound enzyme system contained highly reactive sulfhydryl groups essential for activity. The enzyme was partially activated by norepinephrine and maximally activated by fluoride. Preliminary incubation with fluoride and Mg++, followed by extensive washing with buffer, gave a preparation which showed high activity without further addition of fluoride. In contrast, prior activation by norepinephrine was not maintained after washing of the enzyme with buffer. It is suggested that adenyl cyclase in higher animals is controlled by specific proteins which are coupled with the enzyme and inhibit its activity. The hormone, through binding to a specific site on the inhibitor, reversibly removes the inhibition. Fluoride appears to counteract the inhibition by a process which is not readily reversible." @default.
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- W1609365613 date "1970-06-01" @default.
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- W1609365613 title "Adenyl Cyclase of Rat Parotid Gland" @default.
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- W1609365613 doi "https://doi.org/10.1016/s0021-9258(18)63044-3" @default.
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