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A suspension of microcrystals of phosphoglucomutase in 60% ammonium sulfate
exhibits a maximal catalytic activity in substrate-velocity studies that is
about 0.2 of that obtained with the soluble enzyme under the same conditions.
The apparent Michaelis constants for the reaction in the crystal phase are
altered to an even smaller extent, relative to that in solution, although the
parameters for the monophosphate and bisphosphate are increased more than 3 and
more than 5 orders of magnitude, respectively, by the sulfate present. The
compatibility of larger crystals with a reaction that constitutes part of the
catalytic process also is demonstrated.
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