Similar affinities of ADP and ATP for G‐actin at physiological salt concentrations

FEBS Letters

Wanger, Michael¹  Wegner, Albrecht¹ 

[1]Institut für Physiologische Chemie I, Ruhruniversität Bochum, Universitätsstraβe 150, D-4630 Bochum 1, FRG

关键词: Actin;    1-N6-Ethenoadenosine 5′-triphosphate;    Fluorescence;    Nucleotide exchange;    Equilibrium constant;    ATP;    adenosine 5'-triphosphate;    ADP;    adenosine 5'-diphosphate;    ε-ATP;    1-N 6-ethenoadenosine 5'-triphosphate;    NEM;    N-ethylmaleimide;    PEI;    polyethylenimine;    Tris;    tris (hydroxymethyl)-aminomethane;    EGTA;    ethyleneglycol-bis-(β-aminoethyl ether)-N;    N;    N';    N'-tetraacetic acid;   

DOI  :  10.1016/0014-5793(83)81059-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The equilibrium constant for the exchange of ATP and ADP at G-actin was determined by fluorimetric titration of G-actin-bound ε-ATP by ATP or ADP. The affinity of ATP for G-actin was found to be only about 3-fold higher than the affinity of ADP for G-actin at 37°C, pH 7.5 and physiologically relevant salt concentrations (100 mmol K⁺/l, 0.8 mmol Mg²⁺/l, <0.01 mmol Ca²⁺/l).

【 授权许可】

Unknown