核苷酸和二价阳离子与兔肌浆网中钙镁离子依赖性三磷酸腺苷酶的结合。
The binding of nucleotides and bivalent cations to the calcium-and-magnesium ion-dependent adenosine triphosphatase from rabbit muscle sarcoplasmic reticulum.
作者信息
Yates D W, Duance V C
出版信息
Biochem J. 1976 Dec 1;159(3):719-28. doi: 10.1042/bj1590719.
Abstract
The binding of MgATP to purified Ca2+Mg2+-dependent adenosine triphosphatase from rabbit muscle sarcoplasmic reticulum was studied by using a flow-dialysis method. Phosphoryl-enzyme formation and catalytic activity were also measured, and all three processes demonstrated negative co-operativity, with half-saturation of all three parameters at a MgATP concentration of 40-50muM, and a Hill coefficient (h) of 0.8. The variation of the binding constant with with pH was measured and showed tighter binding of MgATP with increasing pH over the range 6.8-8.5. Binding parameters for ATP analogues were also measured. The binding of Ca2+ in the presence and absence of ATP analogues gave half saturation at a Ca2+ concentration of 1.2-1.3muM. Hill plots of Ca2+-binding data gave a slope of 0.8. These results show that the binding of MgATP and Ca2+ can occur in a random manner, with neither substrate influencing the affinity of the enzyme for the other.
摘要
采用流动透析法研究了MgATP与兔肌浆网纯化的Ca2+Mg2+依赖性三磷酸腺苷酶的结合。还测定了磷酸化酶的形成和催化活性，所有这三个过程均表现出负协同性，在MgATP浓度为40 - 50μM时，所有三个参数的半饱和状态以及希尔系数（h）为0.8。测定了结合常数随pH的变化，结果表明在6.8 - 8.5范围内，随着pH升高，MgATP与酶的结合更紧密。还测定了ATP类似物的结合参数。在有和没有ATP类似物存在的情况下，Ca2+的结合在Ca2+浓度为1.2 - 1.3μM时达到半饱和。Ca2+结合数据的希尔图斜率为0.8。这些结果表明，MgATP和Ca2+的结合可以随机方式发生，两种底物均不影响酶对另一种底物的亲和力。
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