Abstract
Pig-spleen acid α- D-glucosidase, when purified over 2000-fold, has a molecular weight of ≈ 106,000 and is homogeneous by disc-gel electrophoresis. The enzyme splits reducing, α- D-glucosyl disaccharides and almost completely degrades dextrans that contain (1→3)- and (1→6)-linkages. Dextrans containing (1→2)-linkages are only partially hydrolysed. The kinetic parameters for the acid α- D-glucosidase were obtained by using oligo- and poly-saccharide substrates. Variation of pH, temperature, and inhibitors caused changes in the activity of the acid α- D-glucosidase towards oligo- and poly-saccharide substrates. These results support the earlier suggestion that the enzyme has multiple substrate-binding sites.
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