RABBIT SKELETAL-MUSCLE F-ACTIN CAN BE STABLE AT LOW IONIC-STRENGTH, PROVIDED TRACE AMOUNTS OF CA2+ ARE ABSENT

被引：22

作者：

AVISSAR, N

KAMINSKY, E

LEIBOVICH, SJ

OPLATKA, A

机构：

[1] TEL AVIV UNIV, BEILINSON MED CTR, SCH MED, ROGOFF WELLCOME MED RES INST, PETAH TIKVA, ISRAEL

[2] WEIZMANN INST SCI, DEPT BIOL ULTRASTRUCT, REHOVOT 76100, ISRAEL

[3] WEIZMANN INST SCI, DEPT POLYMER RES, REHOVOT 76100, ISRAEL

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 577卷 / 02期

关键词：

Ca[!sup]2+[!/sup; F-Actin stability; Ionic strength;

D O I：

10.1016/0005-2795(79)90030-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Addition of low concentrations (0.2-2.0 mM) of EGTA to rabbit skeletal muscle G-actin in the presence of ATP caused an increase in viscosity. The effect was probably due to chelation of Ca2+. EGTA-polymerized actin was sedimented in the ultracentrifuge as a pellet which could be depolymerized in the presence of Ca2+ and then repolymerized. EM indicated the formation of filamentous actin which appears to be somewhat more flexible than F-actin obtained by polymerization with KCl. The EGTA-polymerized actin was dissociated by [bovine pancreatic] DNAase I faster than KCl-polymerized actin. F-Actin can be stable in very low ionic strength media if Ca2+ is removed. For the protein to be present as G-actin only in such media, micromolar concentrations of Ca2+ must be present.

引用

页码：267 / 272

页数：6

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