The molecular basis for charge heterogeneity in human acid alpha-glucosidase.
The molecular basis for charge heterogeneity in human hepatic alpha-glucosidase (alpha-D-glucoside glucohydrolase, EC 3.2.1.20) was determined by analysis of the carbohydrate and polypeptide components of the enzyme. Only small remnants of high mannose chains that contained neither sialic acid nor mannose 6-phosphate were detected in the carbohydrate structure. Four enzymatically active forms of alpha-glucosidase separated by chromatofocusing were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and were found to contain different polypeptides. The absence of charged residues in oligosaccharide chains and variability in the polypeptide subunits of the charge forms of hepatic alpha-glucosidase suggest that charge heterogeneity results from differences in the protein structure of the charge forms. The pattern of differences in the polypeptide subunits suggests that the charge forms for hepatic alpha-glucosidase may be the product of proteolysis.
D004563:Electrochemistry; D005959:Glucosidases / Q000302:isolation & purification*; D006801:Humans; D007525:Isoelectric Focusing; D008099:Liver / Q000201:enzymology; D008247:Lysosomes / Q000201:enzymology; D008970:Molecular Weight; D009844:Oligosaccharides / Q000302:isolation & purification; D010446:Peptide Fragments / Q000302:isolation & purification; D000520:alpha-Glucosidases / Q000302:isolation & purification*
D009844:Oligosaccharides; D010446:Peptide Fragments; D005959:Glucosidases; D000520:alpha-Glucosidases