Partial deglycosylation of alpha subunit modifies sturgeon gonadotropin function.
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.
Zenkevics
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Laboratory of Biochemistry, Institute of Biology, Latvian University, Salaspils. zenkevics@email.lubi.edu.lv
Vose
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Vosekalne
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Bũcena
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D000818:Animals; D002942:Circular Dichroism; D019281:Dimerization; D005399:Fishes / Q000502:physiology*; D006031:Glycosylation; D006065:Gonadotropins, Pituitary / Q000737:chemistry* / Q000502:physiology*; D017433:Protein Structure, Secondary; D021122:Protein Subunits; D011994:Recombinant Proteins / Q000737:chemistry
D006065:Gonadotropins, Pituitary; D021122:Protein Subunits; D011994:Recombinant Proteins