Comparative study of specific alpha-1,2-glucosidase activity toward glucosyl galactosyl hydroxylysine in various animal species.
1. Assay of the activity of alpha-1,2-glucosidase was completed within 10 min using reversed-phase high performance liquid chromatography and purified dansylated glucosyl galactosyl hydroxylysine as the substrate. 2. A comparative study was made on the enzyme activity of liver homogenate from eight animal species, mouse, frog, chicken, rabbit, pig, rat, human, bovine and that of a spinach leaf homogenate. alpha-1,2-glucosidase activity in human and bovine liver was very low, and that of alpha-1,2-glucosidase could not be detected in the spinach homogenate as expected. 3. 1-deoxynojirimycin, a well known potent inhibitor of alpha-1,2-glucosidases which act on the N-glycosidic type carbohydrate chain, also inhibited alpha-1,2-glucosidase acting specificity on glucosyl galactosyl hydroxylysine derived from the collagen molecule.
D000818:Animals; D002023:Bufo bufo; D002417:Cattle; D002645:Chickens; D002851:Chromatography, High Pressure Liquid; D006801:Humans; D006901:Hydroxylysine / Q000031:analogs & derivatives* / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D051379:Mice; D011817:Rabbits; D051381:Rats; D013045:Species Specificity; D013379:Substrate Specificity; D013552:Swine; D000520:alpha-Glucosidases / Q000378:metabolism*
D006901:Hydroxylysine; C001295:glucosylgalactosylhydroxylysine; C038130:glucosyl-galactosyl-hydroxylysine glucohydrolase; D000520:alpha-Glucosidases