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- W2080490845 abstract "The interaction of aldolase with the myofibrillar matrix of rabbit skeletal muscle has been investigated by means of its effect on kinetic parameters for the enzyme-catalyzed cleavage of fructose 1,6-bisphosphate. Involvement of the active site in the enzymic interaction with the thin filament of muscle is indicated, the association constant for competitive inhibition of catalysis (420 000 M−1) being in excellent agreement with the value of 410 000 M−1 obtained under the same conditions (pH 6.8, I 0.16) from partition equilibrium studies of the aldolase-myofibril interaction (Kuter, M.R., Masters, C.J. and Winzor, D.J. (1983) Arch. Biochem. Biophys. 225, 384–389). A second kinetic study, designed to take into greater account the inhibitory effects of substrate and other phosphate-containing metabolites on the interaction of enzyme with myofibrils, has substantiated further the concept of aldolase existing as an equilibrium mixture of cytoplasmic and filament-bound forms in muscle tissue." @default.
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- W2080490845 title "Enzyme kinetic evidence of active-site involvement in the interaction between aldolase and muscle myofibrils" @default.
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- W2080490845 doi "https://doi.org/10.1016/0167-4838(87)90279-2" @default.
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