Degree Type

Dissertation

Date of Award

1987

Degree Name

Doctor of Philosophy

Department

Chemistry

Abstract

Equilibrium constants for the binding of concanavalin A (Con A) to two sugars were determined chromatographically using the protein immobilized on diol-modified silica. In the "reversed-role" mode, 4-methylumbelliferyl (alpha)-D-mannopyranoside (MUM) was the solute chromatographed and mannose was the inhibitor in the mobile phase for the temperature range of 4(DEGREES) to 30(DEGREES)C. Plots of the reciprocal of the capacity factor versus inhibitor concentration were found to be linear. Binding enthalpies for MUM of -7.0 kcal/mol and for mannose of -6.6 kcal/mole were obtained;Rate constants were determined using the "peak-decay" method for MUM, p-nitrophenyl (alpha)-D-mannopyranoside (PNPM) and ovalbumin (OVA) as solutes on the immobilized Con A support. Dissociation rate constants at 25(DEGREES)C for MUM of 1.8 s('-1), for PNPM of 2.6 s('-1), and for OVA of 7.2 x 10('-3) s('-1) were obtained. Enthalpies of reaction were found to be less than those for the faster reaction taking place in solution. Multiple equilibria are probably the cause for this observation.

DOI

https://doi.org/10.31274/rtd-180813-8631

Publisher

Digital Repository @ Iowa State University, http://lib.dr.iastate.edu/

Copyright Owner

Robert Michael Moore

Language

en

Proquest ID

AAI8716798

File Format

application/pdf

File Size

103 pages

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