Previously reported results of equilibrium-partition experiments on the interaction of aldolase with actin-containing filaments [Walsh, Winzor, Clarke, Masters & Morton (1980) Biochem. J. 186, 89-98] have been subjected to a more rigorous theoretical analysis involving consideration of the consequences of cross-linking interactions between enzyme and filament. The experimental results obtained with F-actin-tropomyosin are best described by a model with one binding site per heptameric repeat unit of filament and a value of 39000 M-1 for the site binding constant, k. Similar analyses of the influence of Ca2+ on aldolase binding to F-actin--tropomyosin--troponin substantiate the existence of two equivalent binding sites (k = 14900 M-1) for the enzyme on each repeat unit of the thin filament. The Ca2+-sensitivity of this interaction reflects either a decrease in the strength of aldolase binding to these two sites (k = 8200 M-1) or the elimination of one site.
Research Article|April 01 1981
Binding of aldolase to actin-containing filaments. Quantitative reappraisal of the interactions
Biochem J (1981) 195 (1): 297-299.
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C J Masters, D J Winzor, L W Nichol; Binding of aldolase to actin-containing filaments. Quantitative reappraisal of the interactions. Biochem J 1 April 1981; 195 (1): 297–299. doi: https://doi.org/10.1042/bj1950297
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