一种关于磷酸盐对Ca2+ + Mg2+激活的ATP酶进行磷酸化作用的模型。
A model for the phosphorylation of the Ca2+ + Mg2+-activated ATPase by phosphate.
作者信息
Froud R J, Lee A G
出版信息
Biochem J. 1986 Jul 1;237(1):207-15. doi: 10.1042/bj2370207.
Abstract
We have shown that changes in fluorescence intensity for the Ca2+ + Mg2+-activated ATPase of sarcoplasmic reticulum labelled with fluorescein isothiocyanate following the addition of Ca2+ can give the ratio of the two conformations (E1 and E2) of the ATPase. We show that the fluorescence response to Ca2+ is unaffected by Mg2+, phosphate or K+, implying that these ions bind equally well to the E1 and E2 conformations. A model is presented for phosphorylation of the ATPase by phosphate as a function of pH, Mg2+, K+ and Ca2+.
摘要
我们已经表明，添加钙离子后，用异硫氰酸荧光素标记的肌浆网Ca2+ + Mg2+激活的ATP酶的荧光强度变化能够得出该ATP酶两种构象（E1和E2）的比例。我们发现，对钙离子的荧光反应不受镁离子、磷酸根或钾离子的影响，这意味着这些离子与E1和E2构象的结合能力相同。本文提出了一个关于磷酸根使ATP酶磷酸化的模型，该模型是pH、镁离子、钾离子和钙离子的函数。
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