Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1971 Sep;124(2):301–318. doi: 10.1042/bj1240301

Allotypically related sequences in the Fd fragment of rabbit immunoglobulin heavy chains

L E Mole 1, S A Jackson 1, R R Porter 1, J M Wilkinson 1,*
PMCID: PMC1177145  PMID: 5158495

Abstract

The sequence has been completed of the N-terminal 94 residues of the variable section of the Fd fragment of heavy chains from rabbit immunoglobulin G (IgG) of allotype As1. Most of the sequence of the same section from IgG of allotype Aa3 is also reported. These results, in conjunction with a substantial sequence of the variable region of allotype Aa2 reported elsewhere (Fleischman, 1971), show the presence of 16 positions (including six consecutive positions) in which the residue present correlates with the allotype. No allotype-related sequence variation has been found in the constant section of the Fd fragment. This evidence supports the view that two genes code for the heavy chain and it can be used as evidence in favour of somatic mutation as the origin of the variability in the sequence of the N-terminal section. The evolutionary origin of the `a' locus allotypes of rabbit immunoglobulins remains obscure.

Full text

PDF
301

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Baglioni C. Genetic control of immunoglobulin synthesis. Proc R Soc Lond B Biol Sci. 1970 Dec 1;176(1044):329–346. doi: 10.1098/rspb.1970.0053. [DOI] [PubMed] [Google Scholar]
  2. Benzer S. ON THE TOPOGRAPHY OF THE GENETIC FINE STRUCTURE. Proc Natl Acad Sci U S A. 1961 Mar;47(3):403–415. doi: 10.1073/pnas.47.3.403. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cebra J. J., Steiner L. A., Porter R. R. The partial sequence of two large peptides from the N-terminal half of heavy chains from normal rabbit immunoglobulin G. Biochem J. 1968 Mar;107(1):79–88. doi: 10.1042/bj1070079. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Dixon H. B., Perham R. N. Reversible blocking of amino groups with citraconic anhydride. Biochem J. 1968 Sep;109(2):312–314. doi: 10.1042/bj1090312. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Dubiski S. Immunochemistry and genetics of a "new" allotypic specificity Ae14 of rabbit gamma-G immunoglobulins: recombination in somatic cells. J Immunol. 1969 Jul;103(1):120–128. [PubMed] [Google Scholar]
  6. FEINSTEIN A. CHARACTER AND ALLOTYPY OF AN IMMUNE GLOBULIN IN RABBIT COLOSTRUM. Nature. 1963 Sep 21;199:1197–1199. doi: 10.1038/1991197b0. [DOI] [PubMed] [Google Scholar]
  7. Fruchter R. G., Jackson S. A., Mole L. E., Porter R. R. Sequence studies of the Fd section of the heavy chain of rabbit immunoglobulin G. Biochem J. 1970 Jan;116(2):249–259. doi: 10.1042/bj1160249. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gally J. A., Edelman G. M. Somatic translocation of antibody genes. Nature. 1970 Jul 25;227(5256):341–348. doi: 10.1038/227341a0. [DOI] [PubMed] [Google Scholar]
  9. Hood L., Eichmann K., Lackland H., Krause R. M., Ohms J. J. Rabbit antibody light chains and gene evolution. Nature. 1970 Dec 12;228(5276):1040–1044. doi: 10.1038/2281040a0. [DOI] [PubMed] [Google Scholar]
  10. Kindt T. J., Mandy W. J., Todd C. W. Association of allotypic specificities of group a with allotypic specificities A11 and A12 in rabbit immunoglobulin. Biochemistry. 1970 Apr 28;9(9):2028–2032. doi: 10.1021/bi00811a026. [DOI] [PubMed] [Google Scholar]
  11. Kindt T. J., Todd C. W. Heavy and light chain allotypic markers on rabbit homocytotropic antibody. J Exp Med. 1969 Oct 1;130(4):859–866. doi: 10.1084/jem.130.4.859. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Koshland M. E., Davis J. J., Fujita N. J. Evidence for multiple gene control of a single polypeptide chain: the heavy chain of rabbit immunoglobulin. Proc Natl Acad Sci U S A. 1969 Aug;63(4):1274–1281. doi: 10.1073/pnas.63.4.1274. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Mandy W. J., Todd C. W. Allotypy of rabbit immunoglobulin: an agglutinating specificity. Vox Sang. 1968;14(4):264–270. doi: 10.1111/j.1423-0410.1968.tb04622.x. [DOI] [PubMed] [Google Scholar]
  14. Mäkelä O., Cross A. M. The diversity and specialization of immunocytes. Prog Allergy. 1970;14:145–207. doi: 10.1159/000289379. [DOI] [PubMed] [Google Scholar]
  15. O'Donnell I. J., Frangione B., Porter R. R. The disulphide bonds of the heavy chain of rabbit immunoglobulin G. Biochem J. 1970 Jan;116(2):261–268. doi: 10.1042/bj1160261. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. OUDIN J. Allotypy of rabbit serum proteins. I. Immuno-chemical analysis leading to the individualization of seven main allotypes. J Exp Med. 1960 Jul 1;112:107–124. doi: 10.1084/jem.112.1.107. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Porter R. R. The structure of the heavy chain of immunoglobulin and its relevance to the nature of the antibody-combining site. The Second CIBA Medal Lecture. Biochem J. 1967 Nov;105(2):417–426. doi: 10.1042/bj1050417. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Prahl J. W., Mandy W. J., Todd C. W. The molecular determinants of the A11 and A12 allotypic specificities in rabbit immunoglobulin. Biochemistry. 1969 Dec;8(12):4935–4940. doi: 10.1021/bi00840a042. [DOI] [PubMed] [Google Scholar]
  19. Prahl J. W., Porter R. R. Allotype-related sequence variation of the heavy chain of rabbit immunoglobulin G. Biochem J. 1968 May;107(6):753–763. doi: 10.1042/bj1070753. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. TODD C. W. Allotypy in rabbit 19S protein. Biochem Biophys Res Commun. 1963 May 3;11:170–175. doi: 10.1016/0006-291x(63)90329-2. [DOI] [PubMed] [Google Scholar]
  21. Tang J., Hartley B. S. A diagonal electrophoretic method for selective purification of methionine peptides. Biochem J. 1967 Feb;102(2):593–599. doi: 10.1042/bj1020593. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Tosi S. L., Dubiski S., Mage R. G. Distribution of allotypic specificities A1, A2, A14, and A15 among immunoglobulin G molecules. J Immunol. 1970 Mar;104(3):641–647. [PubMed] [Google Scholar]
  23. Weigert M. G., Cesari I. M., Yonkovich S. J., Cohn M. Variability in the lambda light chain sequences of mouse antibody. Nature. 1970 Dec 12;228(5276):1045–1047. doi: 10.1038/2281045a0. [DOI] [PubMed] [Google Scholar]
  24. Wilkinson J. M. A method for purifying methionine-containing peptides by radioactive labelling. FEBS Lett. 1969 Aug;4(3):170–172. doi: 10.1016/0014-5793(69)80226-7. [DOI] [PubMed] [Google Scholar]
  25. Wilkinson J. M., Press E. M., Porter R. R. The N-terminal sequence of the heavy chain of rabbit immunoglobulin IgG. Biochem J. 1966 Aug;100(2):303–308. doi: 10.1042/bj1000303. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Wilkinson J. M. Variation in the N-terminal sequence of heavy chains of immunoglobulin G from rabbits of different allotype. Biochem J. 1969 Apr;112(2):173–185. doi: 10.1042/bj1120173. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Wu T. T., Kabat E. A. An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity. J Exp Med. 1970 Aug 1;132(2):211–250. doi: 10.1084/jem.132.2.211. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES