Abstract
The Interaction of Muscle Phosphorylase with Soluble Antibody Fragments
Highlights
Low molecular weight substrates were able to reach the catalytic sites of the enzymeantibody complex, whereas large molecular weight substrates were hindered from access to the ribonuclease sites
It is quite plausible that the reaction of an enzyme antigen with a divalent antibody, which leads to the formation of aggregates, may reduce the chances of a macromolecular substrate reaching the catalytic site
It was not known at the time this study was initiated that this applies to an enzyme combined with univalent antibody fragments, which cannot form aggregates with the antigen
Summary
B, the molar excess of inhibitor to enzyme was 8O:l.111, A and B, are the “uninhibited” controls.Freshly prepared enzyme was used.This is in contrast to the Ki values for aged and fresh phosphorylase, which were not very different. B, the molar excess of inhibitor to enzyme was 8O:l. 111, A and B, are the “uninhibited” controls. This is in contrast to the Ki values for aged and fresh phosphorylase, which were not very different. It appears that fewer antibody molecules have to be bound to an unst.able enzyme for inactivation to occur. In the “protected” enzyme, on the other hand, one might say that fewer antibody molecules can be bound to sites which affect the activity of the enzyme. An explanation for the latter observation will be given below
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Published Version
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