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镧系离子和Cd2+在调节磷酸化酶激酶时能够替代Ca2+。

Lanthanide ions and Cd2+ are able to substitute for Ca2+ in regulating phosphorylase kinase.

作者信息

Sotiroudis T G

出版信息

Biochem Int. 1986 Jul;13(1):59-64.

PMID:3092828
Abstract

Trivalent lanthanide ions and Cd2+ were found to mimic effectively the stimulatory action of Ca2+ on rabbit muscle phosphorylase kinase. In the range of concentrations tested, Cd2+ and lanthanides (Tb3+, Gd3+, Pr3+, Ce3+) could substitute for Ca2+ in activating the enzyme to about 60% and 70% respectively of the maximal level seen with Ca2+, at pH 8.2. The effect induced by Cd2+ was biphasic (stimulation followed by inhibition with increasing metal cation concentration). Similar results were obtained at pH 6.8. Cd2+ and Tb3+ were also able to replace Ca2+ required for the stimulation of phosphorylase kinase activity at pH 8.2 by exogenous calmodulin. Maximal stimulation induced by calmodulin in presence of Cd2+ was significantly higher than that in presence of Ca2+ or Tb3+.

摘要

已发现三价镧系离子和Cd2+能有效模拟Ca2+对兔肌肉磷酸化酶激酶的刺激作用。在测试浓度范围内,在pH 8.2时,Cd2+和镧系元素(Tb3+、Gd3+、Pr3+、Ce3+)可分别替代Ca2+,将该酶激活至Ca2+激活时最大水平的约60%和70%。Cd2+诱导的效应呈双相性(随着金属阳离子浓度增加,先刺激后抑制)。在pH 6.8时也得到了类似结果。Cd2+和Tb3+还能够替代pH 8.2时外源性钙调蛋白刺激磷酸化酶激酶活性所需的Ca2+。钙调蛋白在Cd2+存在下诱导的最大刺激显著高于在Ca2+或Tb3+存在下的最大刺激。

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