Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1972 May;127(5):757–765. doi: 10.1042/bj1270757

The oligosaccharide units of rabbit immunoglobulin G. Multiple carbohydrate attachment sites

M W Fanger 1, D G Smyth 1
PMCID: PMC1178785  PMID: 4672801

Abstract

The carbohydrate structure of rabbit immunoglobulin G isolated from pooled sera was investigated. Amino sugar analysis of fragments of the molecule allowed three oligosaccharides to be located at separate sites on the H-chain. The corresponding glycopeptides were isolated. The average composition of the C1-oligosaccharide was 2 glucosamine, 1 mannose and 2 galactose residues. It appeared to be present in approx. 15% of the H-chains; the carbohydrate was coupled through the amide group of asparagine in a peptide containing asparagine, glycine and threonine within the Fd fragment of the molecule. The average composition of the C2-oligosaccharide was 1 galactosamine, 1 galactose and either 1 or 2 sialic acid residues. It was present on approx. 40% of the H-chains and was attached glycosidically to the OH group of threonine in a peptide Ser-Lys-Pro-Thr-Cys-Pro-Pro-Glu-Leu in the hinge region of the molecule. The average composition of the C3-oligosaccharide was 5 glucosamine, 2 galactose, 5 mannose, 1 fucose and 1 sialic acid residue. It appeared to be present in all the H-chains and was linked through the amide group of asparagine in a peptide Gln-Gln-Phe-Asn-Ser-Thr-Ile-Arg within the Fc fragment of the molecule.

Full text

PDF
757

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Cebra J. J., Steiner L. A., Porter R. R. The partial sequence of two large peptides from the N-terminal half of heavy chains from normal rabbit immunoglobulin G. Biochem J. 1968 Mar;107(1):79–88. doi: 10.1042/bj1070079. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Clamp J. R., Bhatti T., Chambers R. E. The determination of carbohydrate in biological materials by gas-liquid chromatography. Methods Biochem Anal. 1971;19:229–344. doi: 10.1002/9780470110386.ch3. [DOI] [PubMed] [Google Scholar]
  3. Clamp J. R., Dawson G., Hough L. The simultaneous estimation of 6-deoxy-L-galactose (L-fucose), D-mannose, D-galactose, 2-acetamido-2-deoxy-D-glucose (N-acetyl-D-glucosamine) and N-acetylneuraminic acid (sialic acid) in glycopeptides and glycoproteins. Biochim Biophys Acta. 1967 Nov 28;148(2):342–349. doi: 10.1016/0304-4165(67)90129-8. [DOI] [PubMed] [Google Scholar]
  4. FLEISCHMAN J. B., PORTER R. R., PRESS E. M. THE ARRANGEMENT OF THE PEPTIDE CHAINS IN GAMMA-GLOBULIN. Biochem J. 1963 Aug;88:220–228. doi: 10.1042/bj0880220. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. FRANKLIN E. C. Structural units of human 7S gamma globulin. J Clin Invest. 1960 Dec;39:1933–1941. doi: 10.1172/JCI104218. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fanger M. W., Smyth D. G. The determination of glucosamine and galactosamine. Anal Biochem. 1970 Apr;34(2):494–499. doi: 10.1016/0003-2697(70)90134-x. [DOI] [PubMed] [Google Scholar]
  7. Fanger M. W., Smyth D. G. The oligosaccharide units of rabbit immunoglobulin G. Asymmetric attachment of C2-oligosaccharide. Biochem J. 1972 May;127(5):767–774. doi: 10.1042/bj1270767. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Givol D., De Lorenzo F. The position of various cleavages of rabbit immunoglobulin G. J Biol Chem. 1968 Apr 25;243(8):1886–1891. [PubMed] [Google Scholar]
  9. Hong R., Nisonoff A. Relative labilities of the two types of interchain disulfide bond of rabbit gamma G-immunoglobulin. J Biol Chem. 1965 Oct;240(10):3883–3891. [PubMed] [Google Scholar]
  10. Mage M. G., Harrison E. T. A comparison of the labile disulfide bonds of rabbit gamma-G-immunoglobulin fragments. Arch Biochem Biophys. 1966 Mar;113(3):709–717. doi: 10.1016/0003-9861(66)90252-9. [DOI] [PubMed] [Google Scholar]
  11. Mole L. E., Jackson S. A., Porter R. R., Wilkinson J. M. Allotypically related sequences in the Fd fragment of rabbit immunoglobulin heavy chains. Biochem J. 1971 Sep;124(2):301–318. doi: 10.1042/bj1240301. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. NISONOFF A., WISSLER F. C., LIPMAN L. N., WOERNLEY D. L. Separation of univalent fragments from the bivalent rabbit antibody molecule by reduction of disulfide bonds. Arch Biochem Biophys. 1960 Aug;89:230–244. doi: 10.1016/0003-9861(60)90049-7. [DOI] [PubMed] [Google Scholar]
  13. NOLAN C., SMITH E. L. Glycopeptides. II. Isolation and properties of glycopeptides from rabbit gamma-globulin. J Biol Chem. 1962 Feb;237:446–452. [PubMed] [Google Scholar]
  14. PORTER R. R. The hydrolysis of rabbit y-globulin and antibodies with crystalline papain. Biochem J. 1959 Sep;73:119–126. doi: 10.1042/bj0730119. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. ROSEVEAR J. W., SMITH E. L. Glycopeptides. I. Isolation and properties of glycopeptides from a fraction of human gamma-globulin. J Biol Chem. 1961 Feb;236:425–435. [PubMed] [Google Scholar]
  16. Smyth D. S., Utsumi S. Structure at the hinge region in rabbit immunoglobulin-G. Nature. 1967 Oct 28;216(5113):332–335. doi: 10.1038/216332a0. [DOI] [PubMed] [Google Scholar]
  17. Weber P., Winzler R. J. Determination of hexosaminitols by ion-exchange chromatography and its application to alkali-labile glycosidic linkages in glycoproteins. Arch Biochem Biophys. 1969 Feb;129(2):534–538. doi: 10.1016/0003-9861(69)90211-2. [DOI] [PubMed] [Google Scholar]
  18. Weber P., Winzler R. J. Sulfonated amino sugars derived from alkaline sulfite-treated glycoproteins. Arch Biochem Biophys. 1970 Apr;137(2):421–427. doi: 10.1016/0003-9861(70)90458-3. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES