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Structure determination of the disialylated poly-(N-acetyllactosamine)-containingO-linked carbohydrate chains of equine chorionic gonadotropin

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Abstract

The disialylated poly-(N-acetyllactosamine)-containingO-linked oligosaccharide alditols, released by alkaline borohydride treatment of the enzymicallyN-deglycosylated β-subunit of equine chorionic chonadotropin, were purified by fast protein liquid chromatography (FPLC) on Mono Q and analysed by fast ion bombardment mass spectrometry (FAB-MS) and1H-NMR spectroscopy. The identified oligosaccharide alditols have the following structure:

$$\begin{gathered} Neu5Ac\alpha 2 - 3\left[ {Gal\beta 1 - 4GlcNAc\beta 1 - 3} \right]_{0 - 4} Gal\beta 1 - 4GlcNAc\beta 1 - 6 \hfill \\ \begin{array}{*{20}c} { \backslash } \\ { GalNAc - ol} \\ { /} \\ {Neu5Ac\alpha 2 - 3Gal\beta 1 - 3} \\ \end{array} \hfill \\ \end{gathered}$$

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Abbreviations

CG:

chorionic gonadotropin

eCG:

equine chorionic gonadotropin

FAB-MS:

fast atom bombardment mass spectrometry

FID:

free induction decay

FSH:

follicle stimulating hormone

FPLC:

fast protein liquid chromatography

GLC:

gas liquid chromatography

Hex:

hexose

HexNAc:

N-acetylhexosamine

LH:

luteinizing hormone

NAc:

N-acetyl

Neu4,5Ac2 :

N-acetyl-4-O-acetylneuraminic acid

PNGase-F:

peptide-N 4-(N-acetyl-β-glycosaminyl)asparagine amidase F

WEFT:

water eliminated Fourier transform

References

  1. Murphy BD, Martinuk SD (1991)Endocrine Reviews 12:27–44.

    Google Scholar 

  2. Christakos S, Bahl OP (1979)J Biol Chem 254:4253–61.

    Google Scholar 

  3. Bousfield GR, Sugino H, Ward DN (1985)J Biol Chem 260:9531–33.

    Google Scholar 

  4. Sugino H, Bousfield GR, Moore WT Jr, Ward DN (1987)J Biol Chem 262:8603–9.

    Google Scholar 

  5. Damm JBL, Hård K, Kamerling JP, Van Dedem GWK, Vliegenthart JFG (1990)Eur J Biochem 189:175–83.

    Google Scholar 

  6. Kamerling JP, Damm JBL, Hård K, Van Dedem GWK, De Boer W, Vliegenthart JFG (1990) InGlycoprotein Hormones (Chin WW, Boime I, eds) pp. 123–36. Norwell, MA: Serono.

    Google Scholar 

  7. Bahl OP, Anumula KR (1986)Fed Proc 45:1818.

    Google Scholar 

  8. Damm JBL, Kamerling JP, Van Dedem GWK, Vliegenthart JFG (1987)Glycoconjugate J 4:129–44.

    Google Scholar 

  9. Kamerling JP, Vliegenthart JFG (1989) InClinical Biochemistry; Principles, Methods, Applications. Vol. 1,Mass Spectrometry (Lawson AM, ed) pp. 175–263. Berlin: Walter de Gruyter.

    Google Scholar 

  10. Ciucanu I, Kerek F (1984)Carbohydr Res 131:209–17.

    Google Scholar 

  11. York WS, Darvill AG, McNeil M, Stevenson TT, Albersheim P (1986)Methods Enzymol 118:3–40.

    Google Scholar 

  12. Vliegenthart JFG, Dorland L, Van Halbeek H (1983)Adv. Carbohydr Chem Biochem 41:209–374.

    Google Scholar 

  13. Hård K, Van Zadelhoff G, Moonen P, Kamerling JP, Vliegenthart JFG (1992)Eur J Biochem 209:895–915.

    Google Scholar 

  14. Dell A (1987)Adv Carbohydr Chem Biochem 45:19–72.

    Google Scholar 

  15. Kamerling JP, Vliegenthart JFG (1992)Biol Magn Reson 10:1–194.

    Google Scholar 

  16. Hounsell EF, Feeney J, Scudder P, Tang PW, Feizi T (1986)Eur J Biochem 157:375–84.

    Google Scholar 

  17. Hokke CH, Kamerling JP, Van Dedem GWK, Vliegenthart JFG (1991)FEBS Lett 286:18–24.

    Google Scholar 

  18. Hokke CH (1993)PhD Thesis, Utrecht University.

  19. Maemura K, Fukuda M (1992)J Biol Chem 267:24379–86.

    Google Scholar 

  20. Dennis JW (1993)Glycobiology 3:91–93.

    Google Scholar 

  21. Anumula KR, Bahl OP (1986)Fed Proc 45:1843.

    Google Scholar 

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Authors and Affiliations

  1. Bijvoet Center, Department of Bio-Organic Chemistry, Utrecht University, PO Box 80.075, NL-3508 TB, Utrecht, The Netherlands

    Cornelis H. Hokke, Marc J. H. Roosenboom, Johannis P. Kamerling & Johannes F. G. Vliegenthart

  2. Department of Mass Spectrometry, Utrecht University, PO Box 80.083, NL-3508 TB, Utrecht, The Netherlands

    Jane E. Thomas-Oates

Authors
  1. Cornelis H. Hokke
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  2. Marc J. H. Roosenboom
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  3. Jane E. Thomas-Oates
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  4. Johannis P. Kamerling
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  5. Johannes F. G. Vliegenthart
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Hokke, C.H., Roosenboom, M.J.H., Thomas-Oates, J.E. et al. Structure determination of the disialylated poly-(N-acetyllactosamine)-containingO-linked carbohydrate chains of equine chorionic gonadotropin. Glycoconjugate J 11, 35–41 (1994). https://doi.org/10.1007/BF00732430

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  • DOI: https://doi.org/10.1007/BF00732430

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