EsturgeonV1, PubMed, Corpus, bibRecord, 000713

Characterization of serum immunoglobulins in a chondrostean fish, Acipenser baeri.

Identifieur interne : 000713 ( PubMed/Corpus ); précédent : 000712; suivant : 000714

Characterization of serum immunoglobulins in a chondrostean fish, Acipenser baeri.

Auteurs : S. Partula ; J. Charlemagne

Source :

Developmental and comparative immunology [ 0145-305X ]

RBID : pubmed:8299850

English descriptors

KwdEn :
- Amino Acid Sequence, Animals, Electrophoresis, Polyacrylamide Gel (veterinary), Fishes (immunology), Immunoblotting (veterinary), Immunoelectrophoresis (veterinary), Immunoglobulins (blood), Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase, Molecular Sequence Data, Sequence Homology, Amino Acid.
MESH :
- chemical , blood : Immunoglobulins.
- immunology : Fishes.
- veterinary : Electrophoresis, Polyacrylamide Gel, Immunoblotting, Immunoelectrophoresis.
- Amino Acid Sequence, Animals, Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase, Molecular Sequence Data, Sequence Homology, Amino Acid.

Abstract

The euglobulin fraction of sturgeon (Acipenser baeri) serum was analyzed using electrophoretic and immunoblotting techniques. The major protein of this fraction is an IgM-like molecule composed of equimolar 70-kDa glycosylated H chains and 26-30 kDa L chains. In the absence of a reducing agent, the L and H polypeptides may form (mu 2L2)n high molecular weight polymers, mu 2L2 170-kDa units or L2 dimers. These different bonding patterns suggest some structural heterogeneity in the distribution of cysteine residues along the sturgeon Ig chains. The H chain N-terminal sequence indicates significant homologies with the conserved VHIII subgroup. Heavy chains antigenically different from the 70-kDa H chain were not detected, suggesting that IgM is the only Ig class synthesized by this sturgeon species.

PubMed: 8299850

Links to Exploration step

pubmed:8299850

Le document en format XML

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<author><name sortKey="Partula, S" sort="Partula, S" uniqKey="Partula S" first="S" last="Partula">S. Partula</name>
<affiliation><nlm:affiliation>Université Pierre et Marie Curie and CNRS (URA 1135), Groupe d'Immunologie Comparée, Paris, France.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Charlemagne, J" sort="Charlemagne, J" uniqKey="Charlemagne J" first="J" last="Charlemagne">J. Charlemagne</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Characterization of serum immunoglobulins in a chondrostean fish, Acipenser baeri.</title>
<author><name sortKey="Partula, S" sort="Partula, S" uniqKey="Partula S" first="S" last="Partula">S. Partula</name>
<affiliation><nlm:affiliation>Université Pierre et Marie Curie and CNRS (URA 1135), Groupe d'Immunologie Comparée, Paris, France.</nlm:affiliation>
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<author><name sortKey="Charlemagne, J" sort="Charlemagne, J" uniqKey="Charlemagne J" first="J" last="Charlemagne">J. Charlemagne</name>
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<series><title level="j">Developmental and comparative immunology</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Electrophoresis, Polyacrylamide Gel (veterinary)</term>
<term>Fishes (immunology)</term>
<term>Immunoblotting (veterinary)</term>
<term>Immunoelectrophoresis (veterinary)</term>
<term>Immunoglobulins (blood)</term>
<term>Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase</term>
<term>Molecular Sequence Data</term>
<term>Sequence Homology, Amino Acid</term>
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<keywords scheme="MESH" type="chemical" qualifier="blood" xml:lang="en"><term>Immunoglobulins</term>
</keywords>
<keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Fishes</term>
</keywords>
<keywords scheme="MESH" qualifier="veterinary" xml:lang="en"><term>Electrophoresis, Polyacrylamide Gel</term>
<term>Immunoblotting</term>
<term>Immunoelectrophoresis</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase</term>
<term>Molecular Sequence Data</term>
<term>Sequence Homology, Amino Acid</term>
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<front><div type="abstract" xml:lang="en">The euglobulin fraction of sturgeon (Acipenser baeri) serum was analyzed using electrophoretic and immunoblotting techniques. The major protein of this fraction is an IgM-like molecule composed of equimolar 70-kDa glycosylated H chains and 26-30 kDa L chains. In the absence of a reducing agent, the L and H polypeptides may form (mu 2L2)n high molecular weight polymers, mu 2L2 170-kDa units or L2 dimers. These different bonding patterns suggest some structural heterogeneity in the distribution of cysteine residues along the sturgeon Ig chains. The H chain N-terminal sequence indicates significant homologies with the conserved VHIII subgroup. Heavy chains antigenically different from the 70-kDa H chain were not detected, suggesting that IgM is the only Ig class synthesized by this sturgeon species.</div>
</front>
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<DateCreated><Year>1994</Year>
<Month>03</Month>
<Day>04</Day>
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<DateCompleted><Year>1994</Year>
<Month>03</Month>
<Day>04</Day>
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<DateRevised><Year>2003</Year>
<Month>11</Month>
<Day>14</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">0145-305X</ISSN>
<JournalIssue CitedMedium="Print"><Volume>17</Volume>
<Issue>6</Issue>
<PubDate><MedlineDate>1993 Nov-Dec</MedlineDate>
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<Title>Developmental and comparative immunology</Title>
<ISOAbbreviation>Dev. Comp. Immunol.</ISOAbbreviation>
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<ArticleTitle>Characterization of serum immunoglobulins in a chondrostean fish, Acipenser baeri.</ArticleTitle>
<Pagination><MedlinePgn>515-24</MedlinePgn>
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<Abstract><AbstractText>The euglobulin fraction of sturgeon (Acipenser baeri) serum was analyzed using electrophoretic and immunoblotting techniques. The major protein of this fraction is an IgM-like molecule composed of equimolar 70-kDa glycosylated H chains and 26-30 kDa L chains. In the absence of a reducing agent, the L and H polypeptides may form (mu 2L2)n high molecular weight polymers, mu 2L2 170-kDa units or L2 dimers. These different bonding patterns suggest some structural heterogeneity in the distribution of cysteine residues along the sturgeon Ig chains. The H chain N-terminal sequence indicates significant homologies with the conserved VHIII subgroup. Heavy chains antigenically different from the 70-kDa H chain were not detected, suggesting that IgM is the only Ig class synthesized by this sturgeon species.</AbstractText>
</Abstract>
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<Chemical><RegistryNumber>EC 3.2.1.96</RegistryNumber>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
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<MeshHeading><DescriptorName UI="D015151" MajorTopicYN="N">Immunoblotting</DescriptorName>
<QualifierName UI="Q000662" MajorTopicYN="N">veterinary</QualifierName>
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<MeshHeading><DescriptorName UI="D007136" MajorTopicYN="N">Immunoglobulins</DescriptorName>
<QualifierName UI="Q000097" MajorTopicYN="Y">blood</QualifierName>
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<MeshHeading><DescriptorName UI="D017038" MajorTopicYN="N">Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName>
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Characterization of serum immunoglobulins in a chondrostean fish, Acipenser baeri.

Characterization of serum immunoglobulins in a chondrostean fish, Acipenser baeri.

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