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Na_2SeO_3对血影收缩蛋白(spectrin)与肌动蛋白(actin)相互作用的影响
引用本文:胡勇,杨福愉.Na_2SeO_3对血影收缩蛋白(spectrin)与肌动蛋白(actin)相互作用的影响[J].生物物理学报,1992,8(4):701-705.
作者姓名:胡勇  杨福愉
作者单位:中国科学院生物物理所生物大分子国家重点实验室,北京 100101; 清华大学生物科学与技术系 ,北京 100101
摘    要:Na_2SeO_3不影响肌动蛋白(actin)的聚合,但它可通过与血影收缩蛋白(spectrin)作用而间接促进actin的聚合。Na_2SeO_3的作用具有浓度依赖性:低浓度(0.5-5.0ppm)可提高actin聚合过程的成核速度及延伸速度,高浓度则产生相反的效应。巯基试剂如N-乙基马来酰亚胺(NEM)可消除硒的效应。因此,推测适量的硒可能导致spectrin构象发生一定变化,增强spectrin与actin的结合,降低actin链解聚的倾向性,从而稳定红细胞膜骨架。

关 键 词:血影收缩蛋白  肌动蛋白  红细胞膜

EFFECT OF Na_2SeO_3 ON THE INTERATION OF SPECTRIN WITH ACTIN
Abstract:No obvious effect was observed on the polymerization of actin by Na2SeO3. However, in the presence of human erythrocyte spectrin, Na2SeO3 could markedly enhance the polymerization rate of actin.Such Se effect was concentration -dependent. In the presence of trace amount of Na2SeO3 (0.1-10.0 ppm) both nucleation and elongation rates of actin polymerization were detected, but an increase result appeared only with a Na2SeO3 concentration of 0.5-5.0 ppm. An opposite effect of Na2SeO3 was observed at a higher concentration. We also found that sulfhydryl reagen NEM could eliminate the Se effect. It may deduced that in the presence of an appropriate amount of Na2SeO3 the association of spectrin with actin oligomers, and hence the stabilization of erythrocyte membrane skeleton might be strengthened in consequence of the confor-mational changes of spectrins induced by the interaction of their SH groups with Na2SeO3.
Keywords:Selenium  actin  spectrin  erythrocyte membrane skeleton
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