Warianty tytułu
Języki publikacji
Abstrakty
Chemical deglycosylation (dg) of sturgeon Acipenser gueldenstaedti Br. (alphaGTH) resulted in the loss of 83% of its initial carbohydrate content. It altered also recombinant dgalphaGTH + betaGTH dimer molecule, reducing its immunoreactivity by 30%, and fully blocking the hormonal function. CD spectroscopy showed that deglycosylation led to changes in the secondary structure of dgalphaGTH and in the alpha-beta recombinant. The sugar moiety of sturgeon alphaGTH is suggested to play an important role in maintaining the biological function of the hormone dimer molecule.
Wydawca
Czasopismo
Rocznik
Tom
Numer
Opis fizyczny
p.815-819,fig.
Twórcy
autor
- Latvian University, Salaspils, Latvia
autor
autor
autor
Bibliografia
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- 3. Bahl, Om P., Thotakura, N.R. & Anumula, K. R. (1984) in Hormone Receptors in Growth and Reproduction (Serano Symp. Publ., N.Y., Raven Press) vol. 9, 165-183.
- 4. Rathnam, P. & Saxena, B.B. (1984) in Hormone Receptors in Growth and Reproduction (Sirano Symp. Publ., N.Y., Raven Press) vol. 9, 21-35.
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- 6. Zenkevis, H. (1992) in Fish Gonadotropic Hormone. Isolation and Properties; pp. 27-30, Zinatne Publishers, Riga (in Russian).
- 7. Hennen, G., Prusik, Z. & Maghuin-Rogister, G. (1971) Eur. J. Biochem. 18, 376-383.
- 8. Ouchterlony, O. (1958) Progr. Allergy 5, 1-6.
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- 11. Levvy, G.A. & McAllan, A. (1959) J. Biol. Chem. 73, 125-132.
- 12. Dubois, M., Gilles, K.A., Hamilton, J.K., Rebers, P.A. & Smith, F. (1956) Anal. Chem. 28, 350-356.
- 13. Compton, L.A. & Johnson, W.C., Jr. (1986) Anal. Biochem. 155, 155-167.
- 14. Manavalan, P. & Johnson, W.C., Jr. (1987) Anal. Biochem. 167, 76-85.
- 15. Balasubramanian, D. & Kumar, C. (1976) App. Spectroscopy Rev. 11, 223-286.
- 16. Sreerama, N. & Woody, R.W. (1994) Biochemistry33, 10022-10025.
- 17. Sreerama, N. & Woody, R.W. (1994) J. Mol. Biol. 242, 497-507.
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.agro-article-6d64a954-c48e-4f44-9fe9-2855fac4a9b4