Molecular Sieve Studies of Interacting Protein Systems
Year: 1974
Type: article
Abstract: The behavior of isomerizing solutes on molecular sieve columns has been studied theoretically and experimentally. Solutions of the relevant transport equations predict the shape and movement of solute zones for such systems. An experimental investigation of one such system has been carried out: the reversible unfolding of hen egg lysozyme. Results of this study clearly illustrate the effects of finite reaction kinetics on the shapes of solute profiles. To elucidate the influence of chromatographic parameters on the solute profiles, numerical simulations have also been carried out based on the theoretical expressions derived. From these investigations some guidelines have been formulated to aid the design of optimal chromatographic systems for study of isomerizing proteins. In general the technique is best applied to systems with rate constants less than 3 hour-1.
Source: Journal of Biological Chemistry
Authors: Herbert R. Halvorson, Gary K. Ackers
Institution: University of Virginia
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1494617904
