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pubmed-article:1401901pubmed:abstractTextcDNA clones encoding the H chains of the 7.8S and 5.7S IgY of the White Pekin duck have been isolated and sequenced. The H chain of the 7.8S IgY possesses four C region domains and thus resembles the H chain of chicken IgY with which it shows, in the C region, 54% inferred amino acid sequence identity, and complete conservation of the C region cysteine and tryptophan residues. The H chain of the 5.7S IgY possesses only two C region domains, that are virtually identical to CH1 and CH2 of the 7.8S IgY H chain. Although Southern blot genomic analysis did not resolve whether the two transcripts encoding the H chains of the 7.8S and 5.7S IgY are derived from one or two H chain-encoding genes, the CH 1, 2, 3, and 4 exons are apparently colinear, and no evidence was found for a separate locus in which CH1 and 2 exons were present and CH3 and 4 exons were lacking. The VH domain-encoding sequences of the cDNA for the two IgY H chains showed high similarity in the inferred VH gene (93% nucleotide and 91% inferred amino acid identity) and in the inferred JH segment (89% nucleotide and 93% inferred amino acid identity) but low similarity in the D region (26% nucleotide and 7% inferred amino acid identity). Genomic Southern blot hybridization analysis showed multiple VH-hybridizing sequences represented on up to 20 restriction fragments.lld:pubmed
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pubmed-article:1401901pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:1401901pubmed:articleTitleStructural relationship between the two IgY of the duck, Anas platyrhynchos: molecular genetic evidence.lld:pubmed
pubmed-article:1401901pubmed:affiliationDepartment of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston 29425.lld:pubmed
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pubmed-article:1401901pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
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