Modification of alkaline phosphatases by treatment with glycosidases.
The tissue-specific variants of alkaline phosphatase that are characteristic of human liver and bone are believed to possess identical protein cores; nevertheless, they differ in certain properties such as electrophoretic mobility and stability to heat. Their electrophoretic mobilities are modified by digestion with various glycosidases. Furthermore, the difference in heat stability between them is reduced by treatment with a glycosidase preparation from Trichomonas foetalis. These results are consistent with the view that these enzyme variants differ only in their carbohydrate moieties.
D000469:Alkaline Phosphatase / Q000032:analysis* / Q000145:classification; D001842:Bone and Bones / Q000201:enzymology*; D003208:Concanavalin A / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006026:Glycoside Hydrolases; D006358:Hot Temperature; D006801:Humans; D008099:Liver / Q000201:enzymology*; D009928:Organ Specificity
D003208:Concanavalin A; D000469:Alkaline Phosphatase; D006026:Glycoside Hydrolases