Abstract
The technique of differential sedimentation has been used to examine the titration of rabbit muscle glyceraldehyde-3-phosphate dehydrogenase in D 2O buffer with NAD +. The fractional change in sedimentation coefficient was shown to increase linearly as a function of ligand saturation. An examination of the concentration dependence of the sedimentation coefficients of the apo- and holo-enzymes excluded the possibility of changes in the state of aggregation of the enzyme with ligand binding. It was then possible to interpret the changes in sedimentation coefficient with ligand binding in terms of changes in frictional coefficient, reflecting a contraction in the tetrameric assembly on binding NAD +. The linear relation observed between the degree of ligand saturation and the degree of change in frictional coefficient was consistent with the sequential mechanism of conformational changes.
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