Abstract
The heavy and light chains of pooled antibodies of the hybodont shark,Heterodontus francisci (horned shark), were subjected to amino acid sequence analysis. Yield determinations showed that more than 90% of the available polypeptides in the respective pools were sequenced. The heavy chains were homogeneous in the initial framework segment and showed a sequence homology of approximately 70% with the corresponding region of the more recently evolved nurse shark and a 45% homology with a human myeloma heavy chain. The light chains were less homogeneous and not identifiable as either kappa or lambda chains as known in higher species. The first half-cystine characteristics of the variable domain intrachain disulfide bridge of immunoglobulins was present in the same position (22 for heavy chains; 23 for light chains) in the horned shark as in mammalian species. The sequence analysis also suggested the presence of a hypervariable region in the horned shark light chains. The combined data imply that the antigen-binding function of immunoglobulins is mediated in much the same manner in this primitive shark as in more recently evolved species, including mammals.
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Capra, J.D., Wasserman, R.H., and Kehoe, J.M.: Phylogenetically associated residues within the VHIII subgroup of several mammalian species. Evidence for a “pauci-gene” basis for antibody diversity.J. Exp. Med. 138:410–427, 1973
Frommel, D., Litman, G.W., Finstad, J., and Good, R.A.: The immunoglobulins of the horned shark,Helerodontus francisci. Purification, characterization and structural requirement for antibody activity.J. Immunol. 106:1234–1243, 1971
Gaily, J.A.: Structure of Immunoglobulins.In M. Sela (ed):The Antigens, Vol. I; pp. 161–298, Academic Press, London and New York, 1973
Kehoe, J.M., Bourgois, A., Capra, J.D., and Fougereau, N.: Amino acid sequence of a murine immunoglobulin fragment that possesses complement fixing activity.Biochemistry 13:2499–2504, 1974
Litman, G.W.: Relationship between structure and function of lower vertebrate immunoglobulins.In W.H. Hildemann and A.A. Benedict (eds.):Immunologic Phytogeny; pp. 217–228, Plenum Press, New York, 1975
Sledge, C., Clem, L.W., and Hood, L.: Antibody structure: Amino terminal sequences of nurse shark light and heavy chains.J. Immunol. 112:941–948, 1974
Smithies, O., Gibson, D., Fanning, E.M., Goodfliesh, R.M., Gilman, J.M., and Balluantyne, D.L.: Quantitative procedures for use with the Edman-Begg sequenator. Partial sequences of two unusual immunoglobulin light chains, Rzf and Sac.Biochemistry 10:4912–4921, 1971
Stahl, B.J.:Vertebrate History: Problems in Evolution; p. 185, McGraw-Hill, New York, 1974
Summers, M.R., Smythers, G.W., and Oroszlan, S.: Thin-layer chromatography of subnanomole amounts of phenylthiohydantoin (PTH) amino acids on polyamide sheets.Anal. Biochem. 53:624–628, 1973
van Orden, H.O. and Carpenter, F.H.: Hydrolysis of phenylthiohydantoins of amino acids.Biochem. Biophys. Res. Commun. 14:399–403, 1964
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Kehoe, J.M., Sharon, J., Gerber-Jenson, B. et al. The structure of immunoglobulin variable regions in the horned shark,Heterodontus francisci . Immunogenetics 7, 35–40 (1978). https://doi.org/10.1007/BF01843985
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DOI: https://doi.org/10.1007/BF01843985