Abstract
A thorough study of initial rate data was made on carbamoyl phosphate synthetase from bovine liver. On the basis of the results the order of substrate binding to the enzyme is ATPMg followed by HCO3-, ATPMg and NH4+. A model for the enzymic mechanism is proposed, and the rate equations describing it are presented. Details of the derivation of the initial rate equation for the kinetic mechanism proposed have been deposited as Supplementary Publication at the British Library.
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CITATION STYLE
Elliott, K. R. F., & Tipton, K. F. (1974). Kinetic studies of bovine liver carbamoyl phosphate synthetase. Biochemical Journal, 141(3), 807–816. https://doi.org/10.1042/bj1410807
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