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- W2029855940 abstract "The effects of tonicity were studied on the rate of hydrolysis of ATP by Acanthamoeba sp. cells, isolated mitochondria and microsomes as influenced by pH, Mg, Ca and ageing. The ATP hydrolyzing system of this amoeba and its particulates resembles that of an apyrase rather than an ATPase. Optimal pH's for apyrase are 3.2 for whole cells and microsomes, and 4.6 for mitochondria. Apyrase is activated almost equally well by either Mg or Ca ions. Ageing increased particulate apyrase activity only in mitochondria, not in microsomes, and only at suboptimal pH's, in the warm, and with Mg present. Apyrase activity was stimulated in hypotonie and inhibited in hypertonic media not only in whole cells and mitochondria, but also in microsomes. With whole cells, increases in the Mg or Ca ion concentration and the duration of exposure to these activators increased apyrase activity at all tonicities. The results have been discussed and interpreted with reference to Mg and Ca binding and permeability to apyrase sites. The inhibition of apyrase of whole cells, mitochondria and microsomes is coincident with a decreased K influx transfer coefficient under hypertonic conditions." @default.
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- W2029855940 date "1962-12-01" @default.
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- W2029855940 title "Effects of tonicity and pH on apyrase of Acanthamoeba sp. cells and cell fractions" @default.
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- W2029855940 doi "https://doi.org/10.1016/0014-4827(62)90260-4" @default.
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