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Comparative study of specific alpha-1,2-glucosidase activity toward glucosyl galactosyl hydroxylysine in various
1Department of Biochemistry, School of Medicine, Kitasato University, Kanagawa, Japan.
Abstract:
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.