Nucleotide binding to actin : cation dependence of nucleotide dissociation and exchange rates
作者： H.J. Kinosian , L.A. Selden , J.E. Estes , L.C. Gershman
DOI: 10.1016/S0021-9258(18)52929-X
关键词:
摘要: We have reinvestigated nucleotide binding to actin in order resolve conflicts regarding the mechanism of dissociation and exchange. present evidence that supports a for which tightly bound divalent cation (Ca2+ or Mg2+) directly interacts with nucleotide. The rates ATP ADP from are limited by high affinity vary inversely free Ca2+ Mg2+ concentration. concentration range over attenuation takes place is about 100-fold greater than due much slower association rate constant compared Ca2+. relative versus 200:1 Ca-actin 100 microM [Ca2+], 4:1 Mg-actin [Mg2+]. Actin without has 3-fold ADP. At concentration, exchange on described competitive kinetics.
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