EsturgeonV1, PubMed, Corpus, bibRecord, 000649

Partial deglycosylation of alpha subunit modifies sturgeon gonadotropin function.

Identifieur interne : 000649 ( PubMed/Corpus ); précédent : 000648; suivant : 000650

Partial deglycosylation of alpha subunit modifies sturgeon gonadotropin function.

Auteurs : H. Zenkevics ; V. Vose ; I. Vosekalne ; A. B Cena

Source :

Acta biochimica Polonica [ 0001-527X ] ; 2000.

RBID : pubmed:11310980

English descriptors

KwdEn :
- Animals, Circular Dichroism, Dimerization, Fishes (physiology), Glycosylation, Gonadotropins, Pituitary (chemistry), Gonadotropins, Pituitary (physiology), Protein Structure, Secondary, Protein Subunits, Recombinant Proteins (chemistry).
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

Links to Exploration step

pubmed:11310980

Le document en format XML

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<author><name sortKey="Zenkevics, H" sort="Zenkevics, H" uniqKey="Zenkevics H" first="H" last="Zenkevics">H. Zenkevics</name>
<affiliation><nlm:affiliation>Laboratory of Biochemistry, Institute of Biology, Latvian University, Salaspils. zenkevics@email.lubi.edu.lv</nlm:affiliation>
</affiliation>
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<author><name sortKey="Vose, V" sort="Vose, V" uniqKey="Vose V" first="V" last="Vose">V. Vose</name>
</author>
<author><name sortKey="Vosekalne, I" sort="Vosekalne, I" uniqKey="Vosekalne I" first="I" last="Vosekalne">I. Vosekalne</name>
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<author><name sortKey="B Cena, A" sort="B Cena, A" uniqKey="B Cena A" first="A" last="B Cena">A. B Cena</name>
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<author><name sortKey="Vose, V" sort="Vose, V" uniqKey="Vose V" first="V" last="Vose">V. Vose</name>
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<author><name sortKey="Vosekalne, I" sort="Vosekalne, I" uniqKey="Vosekalne I" first="I" last="Vosekalne">I. Vosekalne</name>
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<author><name sortKey="B Cena, A" sort="B Cena, A" uniqKey="B Cena A" first="A" last="B Cena">A. B Cena</name>
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<term>Glycosylation</term>
<term>Gonadotropins, Pituitary (chemistry)</term>
<term>Gonadotropins, Pituitary (physiology)</term>
<term>Protein Structure, Secondary</term>
<term>Protein Subunits</term>
<term>Recombinant Proteins (chemistry)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Gonadotropins, Pituitary</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Fishes</term>
<term>Gonadotropins, Pituitary</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Circular Dichroism</term>
<term>Dimerization</term>
<term>Glycosylation</term>
<term>Protein Structure, Secondary</term>
<term>Protein Subunits</term>
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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>
</front>
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<DateCreated><Year>2001</Year>
<Month>04</Month>
<Day>19</Day>
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<DateCompleted><Year>2001</Year>
<Month>08</Month>
<Day>16</Day>
</DateCompleted>
<DateRevised><Year>2006</Year>
<Month>11</Month>
<Day>15</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">0001-527X</ISSN>
<JournalIssue CitedMedium="Print"><Volume>47</Volume>
<Issue>3</Issue>
<PubDate><Year>2000</Year>
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<Title>Acta biochimica Polonica</Title>
<ISOAbbreviation>Acta Biochim. Pol.</ISOAbbreviation>
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<ArticleTitle>Partial deglycosylation of alpha subunit modifies sturgeon gonadotropin function.</ArticleTitle>
<Pagination><MedlinePgn>815-9</MedlinePgn>
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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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<MedlineJournalInfo><Country>Poland</Country>
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<MeshHeading><DescriptorName UI="D006031" MajorTopicYN="N">Glycosylation</DescriptorName>
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<MeshHeading><DescriptorName UI="D006065" MajorTopicYN="N">Gonadotropins, Pituitary</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName>
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<MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D021122" MajorTopicYN="N">Protein Subunits</DescriptorName>
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<MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName>
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Partial deglycosylation of alpha subunit modifies sturgeon gonadotropin function.

Partial deglycosylation of alpha subunit modifies sturgeon gonadotropin function.

Source :

English descriptors

Abstract

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki