Tight binding of divalent cations to monomeric actin. Binding kinetics support a simplified model.
نویسندگان
چکیده
منابع مشابه
The Binding of Divalent Cations to Actin.
Great effort has been spent in recent years on the investigation of certain aspects of actin polymerization, such as the dephosphorylation of adenosine triphosphate during G to F transformation (l-6), the mode of interaction of ATP with actin (i-15), and the role of sulfhydryl, histidine, tyrosine, and other groups in the polymerization process (8-10, 12-14, 16-18). It has been found that actin...
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It has been shown previously, using G-actin labeled with N-iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylene-diamine, that Mg2+ induces a conformational change in monomeric G-actin as a consequence of binding to a tight divalent cation binding site (Frieden, C. (1982) J. Biol. Chem. 257, 2882-2886). Using the same fluorescent probe, we show that, subsequent to the Mg2+-induced conformational change, c...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1987
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)61137-8