Michelangeli F, Colyer J, East J M, Lee A G
Department of Biochemistry, University of Southampton, U.K.
Biochem J. 1990 Apr 15;267(2):423-9. doi: 10.1042/bj2670423.
A kinetic model for the Ca2(+) + Mg2(+)-activated ATPase of sarcoplasmic reticulum was presented in a previous paper [Stefanova, Napier, East & Lee (1987) Biochem. J. 245, 723-730]. Here, that model is modified to account for the pH-dependence of ATPase activity and for the effects of Mg2+ on activity at high pH. It is shown that effects of Mg2+ on measurements of ATPase activity as a function of ATP concentration at pH 8.0 and pH 8.5 are consistent with binding of Mg2+ to the Ca2(+)-binding sites on the phosphorylated ATPase, such binding inhibiting dephosphorylation of the ATPase. It is also shown that slow dissociation of Ca2+ from the phosphorylated ATPase is consistent with the previously published model.
前一篇论文[斯特凡诺娃、内皮尔、伊斯特和李(1987年)《生物化学杂志》245卷,723 - 730页]提出了肌浆网Ca2(+) + Mg2(+)激活的ATP酶的动力学模型。在此,对该模型进行修改,以解释ATP酶活性的pH依赖性以及Mg2+在高pH下对活性的影响。结果表明,在pH 8.0和pH 8.5时,Mg2+对作为ATP浓度函数的ATP酶活性测量的影响与Mg2+结合到磷酸化ATP酶的Ca2(+)结合位点一致,这种结合抑制了ATP酶的去磷酸化。还表明,Ca2+从磷酸化ATP酶的缓慢解离与先前发表的模型一致。