Stepwise immobilization of proteins via their glycosylation

J Biochem Biophys Methods. 1981 Jun;4(5-6):309-19. doi: 10.1016/0165-022x(81)90071-3.

Abstract

Glycosyl derivatives of bovine serum albumin in which the glycosyl residue is represented by mono- or disaccharide can be, after periodate oxidation, coupled to polyhydrazides having a macroporous matrix (cross-linked polyacrylamide, bead cellulose). The amount of the linked neoglycoprotein depends not only on the physical structure of the matrix but also on the degree of its substitution with hydrazide groups and on the type and concentration of glycosyl residue in the neoglycoprotein. A high degree of substitution as well as the presence of the D-galactosyl unit both play a positive role. Owing to the fact that the glucosyl unit in disaccharide residues (cellobiosyl, lactosyl) also contributes positively to spacer properties, in the monolactosyl derivative of albumin exhibits good binding properties towards macroporous polyhydrazides. While the high sugar-containing conjugates of glycosyl derivatives of albumin with polyhydrazides are stable for two weeks at pH 6-9, the conjugates of the monolactosyl derivative of albumin can only be stored at pH 7.5. The binding site of albumin immobilization is considered.

MeSH terms

  • Binding Sites
  • Carbohydrates*
  • Cellulose / analogs & derivatives
  • Glycoproteins*
  • Hydrazines
  • Indicators and Reagents
  • Methods
  • Protein Binding
  • Proteins*
  • Serum Albumin, Bovine*

Substances

  • Carbohydrates
  • Glycoproteins
  • Hydrazines
  • Indicators and Reagents
  • Proteins
  • Serum Albumin, Bovine
  • Cellulose