Abstract
Hereditary variants of human serum cholinesterase were exposed to the action of sialidase. The removal of the sialic acid residues had no effect on the kinetic properties of the esterases but greatly affected the electrophoretic mobility. In starch gel, there were no differences between the pseudocholinesterase types whether sialidase-treated or untreated. This observation permits two conclusions: first, the differences between the esterase types must reside in the protein cores, and second, the different variants must possess equal amounts of sialic acid per protein molecule. According to Liddell et al. there is a charge difference between esterase molecules of different type; since this cannot be accounted for by sialic acid content, the distinguishing characteristics are likely due to differences of amino acid composition.
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