Formation and decay of the vanadate complex of the sarcoplasmic reticulum calcium transport protein.

P Medda, W Hasselbach
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Abstract

The calcium free sarcoplasmic reticulum calcium transport ATPase incorporates in the presence of magnesium ions approx. 8 nmol monovanadate per mg protein, indicating the formation of a complex containing one vanadate residue per enzyme molecule. On ligand-removal or dilution, the saturated enzyme complex displays biphasic decay kinetics, while the unsaturated complex slowly dissociates monophasically. -Ligand competition by raising the concentrations of unlabeled vanadate results in a progressive decrease of the dissociation rate of the unsaturated enzyme. The complicated dissociation kinetics indicate a sequential mode of interaction between two ligand binding sites. The one to one stoichiometry of the complex suggests that the two sites are located at adjacent ATPase molecules. -It appears unlikely that the decay of the enzyme, vanadate complex is retarded by the formation of a stable quaternary complex between the enzyme, magnesium, mono- and polyvanadate.

肌浆网钙转运蛋白钒酸盐复合物的形成和衰变。
无钙肌浆网钙转运atp酶在镁离子的存在下结合。每毫克蛋白质含有8 nmol单钒酸盐,表明每个酶分子形成一个含有一个钒酸盐残基的复合物。当配体去除或稀释时,饱和酶复合物表现出两相衰变动力学,而不饱和复合物则缓慢地单相解离。-通过提高未标记钒酸盐浓度的配体竞争导致不饱和酶的解离速率逐渐降低。复杂的解离动力学表明两个配体结合位点之间的相互作用是顺序的。该复合物的一对一化学计量表明,这两个位点位于相邻的atp酶分子上。在酶、镁、单钒酸盐和多钒酸盐之间形成稳定的四元络合物,似乎不太可能延缓酶、钒酸盐络合物的衰变。
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