Characterization of serum immunoglobulins in a chondrostean fish, Acipenser baeri
Identifieur interne : 001B82 ( Main/Curation ); précédent : 001B81; suivant : 001B83Characterization of serum immunoglobulins in a chondrostean fish, Acipenser baeri
Auteurs : Sylvie Partula [France] ; Jacques Charlemagne [France]Source :
- Developmental and Comparative Immunology [ 0145-305X ] ; 1993.
Descripteurs français
- Pascal (Inist)
English descriptors
- KwdEn :
Abstract
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 (μ2L2)n high molecular weight polymers, μ2L2 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.
Url:
DOI: 10.1016/S0145-305X(05)80007-2
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<front><div type="abstract" xml:lang="en">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 (μ2L2)n high molecular weight polymers, μ2L2 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>
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<front><div type="abstract" xml:lang="en">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 (μ2L2)n high molecular weight polymers, μ2L2 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>
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