Partial deglycosylation of alpha subunit modifies sturgeon gonadotropin function. | Zendy

Henriks Zenkevičs | Zendy; Vija Vose | Zendy; I Vosekalne | Zendy; A. Būcena | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Partial deglycosylation of alpha subunit modifies sturgeon gonadotropin function.

Author(s) -

Henriks Zenkevičs,

Vija Vose,

I Vosekalne,

A. Būcena

Publication year - 2000

Publication title -

acta biochimica polonica

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.452

H-Index - 78

eISSN - 1734-154X

pISSN - 0001-527X

DOI - 10.18388/abp.2000_3999

Subject(s) - chemistry , recombinant dna , dimer , sturgeon , protein subunit , biochemistry , alpha (finance) , glycosylation , hormone , stereochemistry , medicine , endocrinology , biology , fish <actinopterygii> , gene , fishery , organic chemistry , construct validity , nursing , patient satisfaction

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research