Attachment of thioglycosides to proteins: enhancement of liver membrane binding.
Thioglycosides of D-galactose, D-glucose, N-acetyl-D-glucosamine, and D-mannose were covalently attached to Aspergillus oryzae alpha-amylase, hen's eggs lysozyme, and bovine serum albumin by amidination, diazo coupling, and amide formation. The binding of the newly formed glycoproteins (neoglycoproteins) to rabbit liver membranes was measured, using asialoorosomucoid as a reference. Attachment of D-galactosides by any of the three methods enhanced binding by several orders of magnitude. Coupling of a comparable number of D-mannosides or N-acetyl-D-glucosaminides had little or no effect. Attachment of D-glucosides also enhanced binding but to a variable extent depending on the method of attachment. Thus, the behavior of neoglycoproteins toward rabbit liver membranes closely paralleled that of serum glycoproteins (Ashwell and Morell, 1974) with respect to sugar specificity.
D000117:Acetylglucosamine / Q000378:metabolism; D000681:Amylases / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D008362:Mannosides / Q000378:metabolism; D009113:Muramidase / Q000378:metabolism; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D011817:Rabbits; D012710:Serum Albumin, Bovine / Q000378:metabolism; D013862:Thiogalactosides / Q000378:metabolism; D013863:Thioglucosides / Q000378:metabolism; D013865:Thioglycosides / Q000378:metabolism*
D006023:Glycoproteins; D008362:Mannosides; D011506:Proteins; D013862:Thiogalactosides; D013863:Thioglucosides; D013865:Thioglycosides; D012710:Serum Albumin, Bovine; D000681:Amylases; D009113:Muramidase; D000117:Acetylglucosamine