Study of the glycosylation of apolipoprotein H

Chem Phys Lipids. 1999 Dec;103(1-2):161-74. doi: 10.1016/s0009-3084(99)00108-5.

Abstract

Apolipoprotein H is a single chain polypeptide composed of 326 amino acids highly glycosylated. Its carbohydrate content is approximately 19% of the molecular weight. We show that it is rich in sialic acid linked alpha (2-6) to galactose or N-acetylgalactosamine. Sialic acid is not alpha (2-3) linked to galactose. Galactose is beta (1-4) linked to N-acetylglucosamine and beta (1-3) linked to N-acetylgalactosamine. Carbohydrate O-linked chains (mainly sialic acid) are alpha (2-6) linked to galactose or N-acetylgalactosamine. Galactose is also organised in O-linked chains and beta (1-4) linked to N-acetylglucosamine and beta (1-3) linked to acetylgalactosamine. Concanavalin A lectin was used to isolate two groups of apolipoprotein H molecules bearing biantennary and truncated hybrids and high mannose and hybrid oligosaccharides. Apolipoprotein H fails to bind lysine-Sepharose. Our results thus show that it presents truncated hybrid or hybrid-type carbohydrate chains which bear few unmasked mannose residues as a terminal sugar. Biochemical analysis of carbohydrate structures conducted on single isoforms separated through IEF revealed that no specific carbohydrate complex is bound to a single isoform.

MeSH terms

  • Chromatography, Affinity
  • Disaccharides / chemistry
  • Electrophoresis, Polyacrylamide Gel
  • Glycoproteins / blood*
  • Glycoproteins / chemistry*
  • Glycoproteins / isolation & purification
  • Glycosylation
  • Humans
  • Oligosaccharides / chemistry*
  • Oligosaccharides / isolation & purification
  • Protein Isoforms / blood
  • Protein Isoforms / chemistry
  • Protein Isoforms / isolation & purification
  • beta 2-Glycoprotein I

Substances

  • Disaccharides
  • Glycoproteins
  • Oligosaccharides
  • Protein Isoforms
  • beta 2-Glycoprotein I