Ca2+ + Mg2+激活的ATP酶中的构象转变以及Ca2+离子的结合
Conformational transitions in the Ca2+ + Mg2+-activated ATPase and the binding of Ca2+ ions.
作者信息
Froud R J, Lee A G
出版信息
Biochem J. 1986 Jul 1;237(1):197-206. doi: 10.1042/bj2370197.
Abstract
We have studied the fluorescence of the Ca2+ + Mg2+-activated ATPase of sarcoplasmic reticulum labelled with fluorescein isothiocyanate. The change in intensity of fluorescein fluorescence caused by addition of Ca2+ to the labelled ATPase can be interpreted in terms of a two-conformation model for the ATPase, one conformation (E1) having a high affinity for Ca2+, the other (E2) a low affinity. Effects of Ca2+ as a function of pH allow an estimate of the effect of pH on the E1/E2 ratio, consistent with kinetic studies. A model is presented for binding of Ca2+ to the ATPase as a function of pH that is consistent both with the data on the E1/E2 equilibrium and with literature data on Ca2+ binding.
摘要
我们研究了用异硫氰酸荧光素标记的肌浆网Ca2+ + Mg2+激活的ATP酶的荧光。向标记的ATP酶中添加Ca2+所引起的荧光素荧光强度变化，可以用ATP酶的双构象模型来解释，一种构象（E1）对Ca2+具有高亲和力，另一种（E2）对Ca2+具有低亲和力。Ca2+作为pH函数的效应可以估算pH对E1/E2比率的影响，这与动力学研究结果一致。提出了一个Ca2+作为pH函数与ATP酶结合的模型，该模型与E1/E2平衡数据以及关于Ca2+结合的文献数据均相符。
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Location and dynamics of a membrane-bound fluorescent hapten. A spectroscopic study.膜结合荧光半抗原的定位与动力学：一项光谱学研究
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Modification of the ATP binding site of the Ca2+ -ATPase from sarcoplasmic reticulum by fluorescein isothiocyanate.异硫氰酸荧光素对肌浆网Ca2+ -ATP酶ATP结合位点的修饰
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