Determination of the individual rate and association constants of the hydrolysis catalysed by serine proteinases by means of added nucleophiles in Eisenthal and Cornish-Bowden coordinates.


It is shown that in the three-step enzyme-catalysed hydrolysis the addition of nucleophile shifts the common intersection point in Eisenthal and Cornish-Bowden coordinates when registering the second product P2. The different points obtained at different nucleophile concentrations are situated on a straight line with intercepts Ks on the Km axis and k3 [E]o… (More)