Abstract

Publisher Summary This chapter presents a numerical analysis of kinetic ligand-binding data along with a set of integrated rate equations for simple one-step binding processes. These expressions apply rigorously to the reactions of ligands with hemoglobin monomers. It also describes numerous integration techniques and various types of procedures that are commonly used in the analysis of kinetic data. The selection of a particular method is often a confusing process because of the myriad of available techniques. In general, the simplest integration routines should be tried first, and only when they are found to be inadequate should more sophisticated routines be employed. One of the major difficulties in the analysis of reversible binding to hemoglobin is the large difference between the first and last ligand-dissociation-rate constants. This is expressed by biphasic time courses at low ligand concentrations where incomplete saturation is achieved. The chapter also describes least-squares fitting procedures.

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