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. 1975 Sep;356(9):1413-44.

[Pattern of antibody structure. The amino acid sequence of a monoclonal immunoglobulin L-chain of lambde-type, subgroup I (Bence-Jones-protein Vor.). A contribution to the elucidation of the origin of antibody specificity (author's transl)]

[Article in German]
  • PMID: 809332

[Pattern of antibody structure. The amino acid sequence of a monoclonal immunoglobulin L-chain of lambde-type, subgroup I (Bence-Jones-protein Vor.). A contribution to the elucidation of the origin of antibody specificity (author's transl)]

[Article in German]
M Engelhard et al. Hoppe Seylers Z Physiol Chem. 1975 Sep.

Abstract

The experiments leading to the determination of the primary strucutre of Bence-Jones-Protein Vor. are reported. The variable part of this immunoglobulin polypeptide chain can easily be identified as a typical representative of subgroup I of the lambde-chains. The constant part is characterized by the Kern- and OZ+ markers. The sequence data of this protein are in complete agreement with the demands of the germ line theroy of antibody formation. To demonstrate the evolutionary origin of the V-henes, a phylohenetic tree of all completely sequenced Vk-, Vlambde-, and VH-chains is constructed. Teh evolutionary rate of immunoglobulins is calculated and compared to that of other protein families.

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