Mechanistic studies on yield function of an immobilized multifunctional catalyst

The purpose of this thesis can be divided into three portions. First of all, initial rates are integrated from differential equations for the single and dual substrate enzymatic reaction by using the GEAR package. The artificial initial rates are used to estimate the limitation of applicability of the Michaelis-Menten equation derived by making the equilibrium assumption. A comparison between Michaelis-Menten and a rate equation based on steady-state assumption is introduced, which is the second portion of the thesis. For the last portion of the thesis a corresponding reactivity with and without immobilization of the enzyme which depends on the orientation of the enzyme is discussed. The formulated model seeks to explain the reaction among plasmin, fibrin, and CYp-antiplasmin from the viewpoint of the orientation of the enzyme in the imm.obilized state.