Purification and some properties of lysosomal alpha-glucosidase of rat liver.
Acid alpha-glucosidase was purified from the lysosomal/mitochondrial fraction of rat liver by acid precipitation, ammonium sulphate precipitation and affinity chromatography on Sephadex G 100, resulting in 17000-fold enrichment from that of the liver homogenate. The molecular weight of the enzyme was estimated to be 125000 from analytical gel filtration experiments. On SDS-polyacrylamide gel electrophoresis the purified enzyme showed only a single band having an apparent molecular weight of about 64000. Based on these results, it is concluded that lysosomal liver alpha-glucosidase consists of two subunits. The discontinuous system of SDS-polyacrylamide gel electrophoresis, however, revealed two closely migrating protein bands suggesting heterogeneity of the enzyme subunits.
D000645:Ammonium Sulfate; D000818:Animals; D002846:Chromatography, Affinity; D005959:Glucosidases / Q000302:isolation & purification*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D008099:Liver / Q000201:enzymology*; D008247:Lysosomes / Q000201:enzymology*; D008930:Mitochondria, Liver / Q000201:enzymology; D008970:Molecular Weight; D011506:Proteins / Q000378:metabolism; D051381:Rats; D000520:alpha-Glucosidases / Q000302:isolation & purification* / Q000378:metabolism
D008024:Ligands; D011506:Proteins; D005959:Glucosidases; D000520:alpha-Glucosidases; D000645:Ammonium Sulfate