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STRUCTURAL RESTRICTION AND SIMILARITIES OF THE LIGHT CHAINS OF ANTIBODIES TO GROUP B STREPTOCOCCAL CARBOHYDRATE PRODUCED IN A SINGLE RABBIT
Author(s) -
Raison R. L.,
Marchalonis J. J.
Publication year - 1977
Publication title -
international journal of immunogenetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.41
H-Index - 47
eISSN - 1744-313X
pISSN - 1744-3121
DOI - 10.1111/j.1744-313x.1977.tb00905.x
Subject(s) - hyperimmunization , antibody , homology (biology) , group a , immunoglobulin light chain , amino terminal , chemistry , peptide sequence , amino acid , biology , biochemistry , genetics , medicine , gene
SUMMARY Comparison of the amino acid compositions, N ‐terminal amino acids and tryptic peptide maps of two L chains (145 LI and 145 LII) derived from antibodies produced in a single rabbit to group B streptococci indicates a high degree of sequence homology of the two chains. Furthermore, comparison of these data with similar analysis of L chains prepared from pooled antibodies to group B streptococci indicates a high degree of V region restriction in the L chains of antibodies elicited by hyperimmunization with streptococci.