Studies on the specificity of rabbit hepatic carbohydrate-binding protein using neoglycoproteins

Publisher Website
Google Scholar
Abstract
The binding of amidinoneoglycoproteins of bovine serum albumin to rabbit liver membranes was measured. Derivatives of bovine serum albumin to which equivalent amounts of .beta.-D-Gal, 6-O-Me-.beta.-D-Gal, .beta.-D-Fuc, .alpha.-L-Ara, .beta.-D-Glc,.beta.-D-Xyl and .beta.-D-GalNAc had been attached bound to the membranes equally well. The attachment of .alpha.-D-Man, .beta.-L-Fuc, .beta.-D-GlcNAc, .beta.-D-allose, 3-O-Me-.beta.-D-Glc and 2-deoxy-.beta.-D-Glc did not promote strong binding. The specificity of binding to the membranes was confirmed by measuring the binding of neoglycoproteins to the purified rabbit hepatic carbohydrate-binding protein immobilized on Sepharose 4B. For binding, neither the 6-OH (D-Fuc) nor the 5-CH2OH (L-Ara; D-Xyl) is required, the 4-OH can be axial (D-Gal; L-Ara) or equatorial (D-Glc; D-Xyl), the 3-OH must be equatorial (D-Glc) not axial (D-All) nor may it be substituted (3-O-Me-D-Glc), the 2-OH must be equatorial (D-Glc) not axial (D-Man) and must be present (2-deoxy-D-Glc), and the 2-OH can be replaced by an equatorial acetamido group if the 4-OH is axial (D-GalNAc) but not if it is equatorial (D-GlcNAc).