Partial amino acid sequences of chicken and turkey immunoglobulin light chains. Homology with mammalian λ chains

J. Andrew Grant, Bob Sanders, Leroy Hood

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

The light chains of normal (heterogeneous) immunoglobulins were isolated from individual chickens and turkeys. A new approach is described for determining the number and approximate ratio of light-chain types present in these species. More than 95 % of the chicken and turkey light chains are of a single type that appear to be homologous to mammalian A chains. On the basis of this homology and the presence of both κ and λ chains in mammals it seems likely that κ and λ chains diverged more than 250 million years ago - prior to the separation of the mammalian and avian evolutionary lines. Peptide studies and Edman degradations of intact normal light chains indicate in both species that there is a single predominant variable region sequence. About one-third of the chicken light-chain sequence has been determined. The partial sequences of peptides isolated from turkey light chains indicate that they differ from the corresponding peptides in chicken light chains in only 2 of a total of 74 residues.

Original languageEnglish (US)
Pages (from-to)3123-3132
Number of pages10
JournalBiochemistry
Volume10
Issue number16
StatePublished - 1971

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Immunoglobulin Light Chains
Amino Acid Sequence
Chickens
Light
Amino Acids
Peptides
Mammals
Immunoglobulins
Degradation

ASJC Scopus subject areas

  • Biochemistry

Cite this

Partial amino acid sequences of chicken and turkey immunoglobulin light chains. Homology with mammalian λ chains. / Andrew Grant, J.; Sanders, Bob; Hood, Leroy.

In: Biochemistry, Vol. 10, No. 16, 1971, p. 3123-3132.

Research output: Contribution to journalArticle

Andrew Grant, J. ; Sanders, Bob ; Hood, Leroy. / Partial amino acid sequences of chicken and turkey immunoglobulin light chains. Homology with mammalian λ chains. In: Biochemistry. 1971 ; Vol. 10, No. 16. pp. 3123-3132.
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