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The effect of ATP concentration on the rate of actin polymerization.

Abstract：

:It was found that the rate of polymerization of G-actin increased with the decrease of ATP concentration. When excess ATP was replaced by chloride through anion-exchange treatment, the extent of actin polymerization did not change provided that the ionic strength was raised immediately after the treatment. In the meantime, the rate of actin polymerization was greatly enhanced after the removal of excess ATP. The rate enhancement was much less when both excess Ca2+ and excess ATP were removed. G-actin with excess ATP replaced by chloride had larger light scattering and showed a "catalytic" effect on the polymerization of normal G-actin. The inhibition of actin polymerization by cytochalasin B in 100 mM KCl was much more obvious for G-actin with excess ATP removed than for normal G-actin. It is suggested that the reduction of excess ATP concentration in a G-actin solution increases the binding of weak-affinity Ca2+ and promotes the formation of oligomeric actin (actin nuclei).

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Fung BM,Eyob E

doi

10.1016/0003-9861(83)90426-5

subject

Has Abstract

pub_date

1983-02-01 00:00:00

pages

370-8

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(83)90426-5

journal_volume

220

pub_type

杂志文章

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