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. 1981 Nov;78(11):7088–7090. doi: 10.1073/pnas.78.11.7088

Organization of the diversity--joining region in rabbit immunoglobulin heavy chains as revealed by cleavage of a specific methionine residue in a100 allotype.

C Tonnelle, P A Cazenave, C Brézin, M Fougereau
PMCID: PMC349200  PMID: 6796967

Abstract

Three anti-micrococcus antibodies of restricted heterogeneity have been isolated from the antisera of homozygous a100/a100 rabbits. Heavy chains contained an unusual methionine residue at position 87 that may correlate with the a100 specificity. From this position, the sequence of a stretch of 35-50 amino acid residues was determined, permitting the definition of variable (V), diversity(D), and joining (J) segments in rabbit Ig heavy chains, with their most probable boundaries. Rabbit D regions so defined appear to be highly variable, both in sequence and in length, which varies, in the heavy chains analyzed, between 6 and 11 residues. The J regions are highly homologous to the mouse J2 segment.

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Selected References

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

  1. Awdeh Z. L., Williamson A. R., Askonas B. A. Isoelectric focusing in polyacrylamide gel and its application to immunoglobulins. Nature. 1968 Jul 6;219(5149):66–67. doi: 10.1038/219066a0. [DOI] [PubMed] [Google Scholar]
  2. Bernard O., Gough N. M. Nucleotide sequence of immunoglobulin heavy chain joining segments between translocated VH and mu constant regions genes. Proc Natl Acad Sci U S A. 1980 Jun;77(6):3630–3634. doi: 10.1073/pnas.77.6.3630. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Brézin C., Cazenave P. A. Allotypy of rabbit immunoglobulins: a fifth allele at the a locus. J Immunol. 1980 Jul;125(1):59–62. [PubMed] [Google Scholar]
  4. Cazenave P. A., Brezin C., Roland J. An allotypic specificity presumably of the a series in rabbit immunoglobulins, different from a1, a2, and a3. Biochem Biophys Res Commun. 1974 Nov 27;61(2):664–670. doi: 10.1016/0006-291x(74)91008-0. [DOI] [PubMed] [Google Scholar]
  5. Cazenave P. A., Brézin C. Study of A100 allotypic specificity of rabbit immunoglobulins: the cross-reactivity between A100, a1 and a3. Eur J Immunol. 1976 Apr;6(4):262–269. doi: 10.1002/eji.1830060406. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. Early P., Huang H., Davis M., Calame K., Hood L. An immunoglobulin heavy chain variable region gene is generated from three segments of DNA: VH, D and JH. Cell. 1980 Apr;19(4):981–992. doi: 10.1016/0092-8674(80)90089-6. [DOI] [PubMed] [Google Scholar]
  8. Fleischman J. B. A partial amino acid sequence in the heavy chain of a rabbit antibody to group C streptococcal carbohydrate. Biochemistry. 1971 Jul 6;10(14):2753–2761. doi: 10.1021/bi00790a016. [DOI] [PubMed] [Google Scholar]
  9. Givol D., Porter R. R. The C-terminal peptide of the heavy chain of the rabbit immunoglobulin IgG. Biochem J. 1965 Dec;97(3):32C–34C. doi: 10.1042/bj0970032c. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Jaton J. C., Braun D. G., Strosberg A. D., Haber E., Morris J. E. Restricted rabbit antibodies: amino acid sequences of rabbit H chains of allotype a1, a2, and a3 in the region 80 to 94. J Immunol. 1973 Dec;111(6):1838–1843. [PubMed] [Google Scholar]
  11. Jaton J. C. Completion of the analysis of the primary structure of the variable domain of a homogeneous rabbit antibody to type III pneumococcal polysaccharide. Biochem J. 1974 Dec;143(3):723–732. doi: 10.1042/bj1430723. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Jaton J. C. The V-region sequence of the H chain from a third rabbit anti-pneumococcal antibody. Biochem J. 1976 Aug 1;157(2):449–459. doi: 10.1042/bj1570449. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Johnstone A. P., Thunberg A. L., Kindt T. J. Homogeneous rabbit immunoglobulin lacking group a allotypes: amino acid sequence analysis of the heavy chain. Biochemistry. 1978 Apr 4;17(7):1337–1344. doi: 10.1021/bi00600a031. [DOI] [PubMed] [Google Scholar]
  14. Kindt T. J. Rabbit immunoglobulin allotypes: structure, immunology, and genetics. Adv Immunol. 1975;21:35–86. doi: 10.1016/s0065-2776(08)60218-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Klapper D. G., Wilde C. E., 3rd, Capra J. D. Automated amino acid sequence of small peptides utilizing Polybrene. Anal Biochem. 1978 Mar;85(1):126–131. doi: 10.1016/0003-2697(78)90282-8. [DOI] [PubMed] [Google Scholar]
  16. Krause R. M. Experimental approaches to homogenous antibody populations. Factors controlling the occurrence of antibodies with uniform properties. Fed Proc. 1970 Jan-Feb;29(1):59–65. [PubMed] [Google Scholar]
  17. Mole L. E., Geier M. D., Koshland M. E. The isolation and characterization of the V-H domain from rabbit heavy chains of different a locus allotype. J Immunol. 1975 May;114(5):1442–1448. [PubMed] [Google Scholar]
  18. Newell N., Richards J. E., Tucker P. W., Blattner F. R. J genes for heavy chain immunoglobulins of mouse. Science. 1980 Sep 5;209(4461):1128–1132. doi: 10.1126/science.6250219. [DOI] [PubMed] [Google Scholar]
  19. 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]
  20. OUDIN J. Allotypy of rabbit serum proteins. II. Relationships between various allotypes: their common antigenic specificity, their distribution in a sample population; genetic implications. J Exp Med. 1960 Jul 1;112:125–142. doi: 10.1084/jem.112.1.125. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. OUDIN J. L'allotypie de certains antigènes protéidiques du sérum. C R Hebd Seances Acad Sci. 1956 May 23;242(21):2606–2608. [PubMed] [Google Scholar]
  22. Pratt D. M., Mole L. E. Sequence studies on the constant region of the Fd sections of rabbit immunoglobulin G of different allotype. Biochem J. 1975 Nov;151(2):337–349. doi: 10.1042/bj1510337. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Roland J., Cazenave P. A. Un motif allotypique probablement de nature glucidique porté par le fragment Fab des IgG de lapin. Ann Immunol (Paris) 1976 Sep-Oct;127(5):633–655. [PubMed] [Google Scholar]
  24. Sakano H., Maki R., Kurosawa Y., Roeder W., Tonegawa S. Two types of somatic recombination are necessary for the generation of complete immunoglobulin heavy-chain genes. Nature. 1980 Aug 14;286(5774):676–683. doi: 10.1038/286676a0. [DOI] [PubMed] [Google Scholar]
  25. Schilling J., Clevinger B., Davie J. M., Hood L. Amino acid sequence of homogeneous antibodies to dextran and DNA rearrangements in heavy chain V-region gene segments. Nature. 1980 Jan 3;283(5742):35–40. doi: 10.1038/283035a0. [DOI] [PubMed] [Google Scholar]
  26. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]

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