Binding of Ca2+ to the calcium adenosinetriphosphatase of sarcoplasmic reticulum.
Binding of Ca2+ to the calcium adenosinetriphosphatase of sarcoplasmic reticulum.
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Ca2 与肌浆网钙腺苷三磷酸酶的结合。
DOI：
10.1021/bi00423a018
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发表时间：
1988
期刊：
影响因子：
2.9
通讯作者：
Jencks,WP
中科院分区：
文献类型：
--
作者：
Petithory,JR;Jencks,WP
材料和方法试剂和实验步骤与之前的论文（Petithory & Jencks, 1988）中描述的相同，除非另有说明。肌浆网囊泡由兔骨骼肌制备，对MacLennan（1970）的方法稍加修改，如前面所述（Khananshvili & Jencks, 1988）。当钙离子载体A23187 （2 μ 1-2 mM的乙醇溶液，2 mL的反应溶液）渗透囊泡时，该制剂以3.5-5.0µ1/（总蛋白-min的^）水解ATP。分离的SRV有98%的密封性，在标准实验中，加入离子载体后，稳态ATP水解率提高了50倍。完整囊泡饱和[Ca2+]和[ATP]的磷酸化酶量为2.0-4.0 nmol/mg总蛋白。
Materials and MethodsReagents and experimental procedures were the same as those describedin a previous paper (Petithory & Jencks, 1988), unless indicated otherwise. Sarcoplasmic reticulum vesicles were prepared from rabbit skeletal muscle by a slight modification of the MacLennan (1970) procedure, as described previously (Khananshvili & Jencks, 1988). The preparations hydrolyzed ATP at 3.5-5.0 µ 1/(^ of total protein-min) when the vesicles were made permeable with the calcium ionophore A23187 (2 µ of 1-2 mM in ethanol for 2 mL of reaction solution). SRV as isolated were~ 98% sealed, as shown by an increase of~50-fold in the steady-state ATP hydrolysis rate upon addition of ionophore in the standard assay. The amount of phosphoenzyme observed with intact vesicles atsaturating [Ca2+] and [ATP] was 2.0-4.0 nmol/mg of total protein.