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Chemical modification of the calcium ion dependent atpase ec 3.6.1.3 of sarcoplasmic reticulum from skeletal muscle part 1 binding of n ethyl maleimide to sarcoplasmic reticulum evidence for sulfhydryl groups in the active site of atpase and for conformational changes induced by adp and atp



Chemical modification of the calcium ion dependent atpase ec 3.6.1.3 of sarcoplasmic reticulum from skeletal muscle part 1 binding of n ethyl maleimide to sarcoplasmic reticulum evidence for sulfhydryl groups in the active site of atpase and for conformational changes induced by adp and atp



Journal of Biochemistry 79(3): 649-654



The time course of binding of N-ethylmaleimide (NEM) to the [rabbit] SR [sarcoplasmic reticulum] was measured at pH 7.5 in the presence of absence of ATP or ADP. Both in the presence and absence of nucleotide, the ATPase [EC 3.6.1.3] activity decreased linearly with increase in the amount of NEM bound to the fragmented SR, and was inhibited almost completely by the binding of 2 mol of NEM/105 g of the SR protein. The amount of NEM incorporated into the ATPase (MW = 105,000) was measured by SDS disc-gel electrophoresis. The ATPase activity was inhibited almost completely by the binding of 2 mol of NEM/mol of ATPase. The rate of binding of NEM to SR decreased by 30-40% in the presence of either ATP or ADP. The concentrations of both ATP and ADP for half-saturation were 0.1-0.2 mM. The effect of nucleotide on the rate of binding of NEM was not changed by the presence of Ca2+ and Mg2+O. Similar effects were also observed even when the SR membranes were solubilized with Triton X-100. One or 2 SH groups are probably located in the active site of the SR ATPase. Addition of ATP and ADP may induce conformational changes.

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Accession: 004938684

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Chemical Modification of the Ca2+-dependent Atpase of Sarcoplasmic Reticulum from Skeletal Muscle. I. Binding of N-Ethylmaleimide to Sarcoplasmic Reticulum: Evidence for Sulfhydryl Groups in the Active Site of Atpase and for Conformational Changes Induced by Adenosine Tri- and Diphosphate1. The Journal of Biochemistry 79(3): 649-654, 1976

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