Relaxation kinetics of glutamate dehydrogenase self-association by pressure perturbation

Publisher Website
Google Scholar
Abstract
The kinetics of self-association for beef liver glutamate dehydrogenase (EC 1.4.1.3) were measured by using pressure perturbation in both the time domain and the frequency domain by monitoring scattered light intensity. The kinetic behavior is consistent with the random self-association model proposed by Thusius et al. The activation volume .DELTA.V for association is estimated to be positive; this provides further corroboration of the molecular mechanism advanced by these authors. A rapid shift in scattered light intensity is due to preferential interaction between the phosphate anion and the protein, proceeding with a positive volume change (2-5 ml/mol of phosphate). A description of the instrument developed for this study is included.

This publication has 0 references indexed in Scilit: