ACTION OF AMYLO-1,6-GLUCOSIDASE ON LOW MOLECULAR WEIGHT SUBSTRATES AND THE ASSAY OF THIS ENZYME IN GLYCOGEN STORAGE DISEASE

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Abstract
Amylo-l,6-glucosidase has been extensively purified from rabbit muscle and has been found to act directly on a singly branched oligosaccharide containing five glucose residues to yield one mole of glucose and one mole of maltotetraose. This low molecular weight substrate has been purified chromatographically from the mixed products of pancreatic a-amylase action on either glycogen or amylopectin and its structure has been investigated. It has been found suitable as a substrate for the assay of the glucosidase in small samples of human liver. This specific assay procedure has been applied to a number of cases of glycogen storage disease, and its usefulness in detecting that type of disease in which there is a lack of the glucosidase has been shown.