Comparative Study of the Sugar Chains of γ-Glutamyltranspeptidases Purified from Rat Liver and Rat AH-66 Hepatoma Cells

摘要: A comparative study using hydrazinolysis has revealed that the oligosaccharide pattern of γ-glutamyltranspeptidase purified from rat AH-66 hepatoma cells is very different enzyme liver. Studies oligosaccharides in each fraction have clarified structural basis difference found sugar chains two enzymes. The liver were all acidic, while 28% those neutral, latter being composed high-mannose-type and complex-type chains. Three prominent differences acidic enzymes: ( a ) complete outer chains, Galβ1→4GlcNAcβ1→, many incomplete without galactose (Gal); b Galβ1→4GlcNAcβ1→Galβ1→4GlcNAcβ1→ group but not enzyme; c more than 40% contain bisect N -acetylglucosamine (GlcNAc) residue which enzyme. Furthermore, total number asparagine-linked one molecule was about 4 times enzyme.