Partial deglycosylation of alpha subunit modifies sturgeon gonadotropin function.
Identifieur interne : 000649 ( PubMed/Curation ); précédent : 000648; suivant : 000650Partial deglycosylation of alpha subunit modifies sturgeon gonadotropin function.
Auteurs : H. Zenkevics [Lettonie] ; V. Vose ; I. Vosekalne ; A. B CenaSource :
- Acta biochimica Polonica [ 0001-527X ] ; 2000.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Gonadotropins, Pituitary, Recombinant Proteins.
- physiology : Fishes, Gonadotropins, Pituitary.
- Animals, Circular Dichroism, Dimerization, Glycosylation, Protein Structure, Secondary, Protein Subunits.
Abstract
Chemical deglycosylation (dg) of sturgeon Acipenser gueldenstaedti Br. (alphaGTH) resulted in the loss of 83% of its initial carbohydrate content. It altered also recombinant dg alphaGTH + 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 dg alphaGTH 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.
PubMed: 11310980
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pubmed:11310980Le document en format XML
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<front><div type="abstract" xml:lang="en">Chemical deglycosylation (dg) of sturgeon Acipenser gueldenstaedti Br. (alphaGTH) resulted in the loss of 83% of its initial carbohydrate content. It altered also recombinant dg alphaGTH + 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 dg alphaGTH 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.</div>
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<Abstract><AbstractText>Chemical deglycosylation (dg) of sturgeon Acipenser gueldenstaedti Br. (alphaGTH) resulted in the loss of 83% of its initial carbohydrate content. It altered also recombinant dg alphaGTH + 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 dg alphaGTH 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.</AbstractText>
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