Studies on the mechanism of action of the histone kinase dependent on adenosine 3′,5′‐monophosphate

Abstract
The transient phase of histone H1 phosphorylation was studied by the quenched-flow method. A minimal kinetic scheme of the above process was proposed. A formal kinetic analysis was given to a 4-step mechanism of the reaction. Computer stimulation of the transient-phase kinetics of H1 phosphorylation and the steady-state kinetics of phosphate transfer from the enzyme phosphoform to histone permitted an estimate of all kinetic constants of the proposed mechanism.

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