Dog and human acid beta-D-galactosidases are structurally similar.
The purification of dog liver acid beta-galactosidase is described. The dog enzyme migrated as a single major band on polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate, with a molecular weight of 60000. Antiserum raised against purified human liver acid beta-galactosidase cross-reacted with beta-galactosidase from dog liver, but not with those from cat liver or Escherichia coli. Tryptic peptide maps of the dog and human acid beta-galactosidases indicate that 21 of the 24 peptides observed were homologous; a similar result was obtained after chymotryptic peptide mapping. We conclude that dog and human acid beta-galactosidases are structurally similar, and that canine GM1 gangliosidosis (acid beta-galactosidase deficiency) is an excellent model for the same disease in man.
D000818:Animals; D002415:Cats; D055598:Chemical Phenomena; D011232:Chemical Precipitation; D002621:Chemistry; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D005696:Galactosidases / Q000302:isolation & purification / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D010446:Peptide Fragments / Q000032:analysis; D013045:Species Specificity; D001616:beta-Galactosidase / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism
D010446:Peptide Fragments; D005696:Galactosidases; D001616:beta-Galactosidase