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S-100a0蛋白刺激从分离的肌浆网囊泡中由钙离子诱导的钙离子释放。

S-100a0 protein stimulates Ca2+-induced Ca2+ release from isolated sarcoplasmic reticulum vesicles.

作者信息

Fanò G, Marsili V, Angelella P, Aisa M C, Giambanco I, Donato R

机构信息

Institute of Cell Biology, Faculty of Sciences, University of Perugia, Italy.

出版信息

FEBS Lett. 1989 Sep 25;255(2):381-4. doi: 10.1016/0014-5793(89)81127-5.

Abstract

S-100a0 protein, the alpha alpha-isoform of the S-100 family, stimulates Ca2+-induced Ca2+ release from terminal cisternae isolated from rat skeletal muscle cells. The stimulatory effect of S-100a0 is maximal at approximately 5 microM S-100a0 and half maximal at approximately 0.1 microM S-100a0, at 1.8 microM free Ca2+ in the presence of 5 mM Mg2+ plus 0.1 M KCl. The effect of the protein on Ca2+-induced Ca2+ release is completely inhibited by the calcium release blocker, ruthenium red.

摘要

S-100a0蛋白,即S-100家族的αα异构体,可刺激从大鼠骨骼肌细胞分离出的终池进行钙诱导的钙释放。在5 mM Mg2+加0.1 M KCl存在的情况下,当游离Ca2+浓度为1.8 microM时,S-100a0的刺激作用在约5 microM S-100a0时达到最大,在约0.1 microM S-100a0时达到最大刺激作用的一半。钙释放阻滞剂钌红可完全抑制该蛋白对钙诱导的钙释放的作用。

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