肌浆网的钙ATP酶受一个钙离子抑制。
The calcium ATPase of sarcoplasmic reticulum is inhibited by one Ca2+ ion.
作者信息
Khananshvili D, Myung J, Kolouch R, Jencks W P
机构信息
Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.
出版信息
FEBS Lett. 1990 Jan 15;260(1):83-4. doi: 10.1016/0014-5793(90)80071-p.
PMID:2137096
Abstract
Inhibition by calcium of the steady-state turnover of the calcium ATPase from sarcoplasmic reticulum of rabbit muscle follows a Hill slope of 0.8 +/- 0.2 (pH 7.0, 0.1 M KCl, varying [Mg2+] and 2 microM A23187 ionophore). It is concluded that dissociation of the two Ca2+ ions from E-P.Ca2 is sequential and that the inhibition arises from the binding of one Ca2+ to A-P.Ca1.
摘要
钙对兔肌肌浆网钙ATP酶稳态周转的抑制作用遵循的希尔斜率为0.8±0.2（pH 7.0，0.1 M KCl，不同的[Mg2+]以及2 microM A23187离子载体）。得出的结论是，两个Ca2+离子从E-P.Ca2解离是相继发生的，并且抑制作用源于一个Ca2+与A-P.Ca1的结合。
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