Effects of Subtilisin Cleavage of Monomeric Actin on Its Nucleotide Binding

The kinetics of ATP exchange on subtilisin-cleaved G-actin was investigated by measuring the fluorescence of 1,N6-ethenoadenosine 5'-triphosphate. The apparent dissociation rate of ATP (k−ATP) was 2.8-fold larger than that of intact G-actin in the presence of 300 μM free Ca2+. Analysis of the d...

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Veröffentlicht in:Journal of biochemistry (Tokyo) 1996-12, Vol.120 (6), p.1104-1110
Hauptverfasser: Ooi, Atsushi, Mihashi, Koshin
Format: Artikel
Sprache:eng
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