Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1977 Oct 1;167(1):255–267. doi: 10.1042/bj1670255

Sequence studies on the heavy chain of rabbit immunoglobulin A of different alpha-locus allotypes.

A P Johnstone, L E Mole
PMCID: PMC1183643  PMID: 412498

Abstract

The amino acid sequence was determined of part of the variable region of heavy chain from rabbit immunoglobulin A of allotypes a1 and a3. Two corrections of the primary sequence of Aa1 gamma-chains are reported; most of the structural correlates of the alpha-locus allotypes are confirmed. The amino acid sequence of the N-terminal 20 residues of alpha-negative molecules was also determined and found to be homologous to the human VhIII subgroup. These molecules are present in a much higher proportion in the alpha-chain pool than in the gamma-chain.

Full text

PDF
255

Selected References

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

  1. Ansari A. A., Carta-Sorcini M., Mage R. G., Appella E. Studies on the structural localization of rabbit H chain allotypic determinants controlled by the a locus. Purification and immunological properties of an immunopeptide bearing a3 allotypic determinants. J Biol Chem. 1976 Nov 10;251(21):6798–6606. [PubMed] [Google Scholar]
  2. Bennett J. C. The amino-terminal sequence of the heavy chain of human immunoglobulin M. Biochemistry. 1968 Oct;7(10):3340–3344. doi: 10.1021/bi00850a005. [DOI] [PubMed] [Google Scholar]
  3. Brauer A. W., Margolies M. N., Haber E. The application of 0.1 M quadrol to the microsequence of proteins and the sequence of tryptic peptides. Biochemistry. 1975 Jul;14(13):3029–3035. doi: 10.1021/bi00684a036. [DOI] [PubMed] [Google Scholar]
  4. Capra J. D., Kehoe J. M. Distribution and association of heavy and light chain variable region subgroups among human IgA immunoglobulins. J Immunol. 1975 Feb;114(2 Pt 1):678–681. [PubMed] [Google Scholar]
  5. Capra J. D., Kehoe J. M. Hypervariable regions, idiotypy, and the antibody-combining site. Adv Immunol. 1975;20:1–40. doi: 10.1016/s0065-2776(08)60205-9. [DOI] [PubMed] [Google Scholar]
  6. Capra J. D., Wasserman R. L., Kehoe J. M. Phylogenetically associated residues within the VH3 subgroup of several mammalian species. Evidence for a "pauci-gene" basis for antibody diversity. J Exp Med. 1973 Aug 1;138(2):410–427. doi: 10.1084/jem.138.2.410. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. 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]
  8. Dreyer W. J., Bennett J. C. The molecular basis of antibody formation: a paradox. Proc Natl Acad Sci U S A. 1965 Sep;54(3):864–869. doi: 10.1073/pnas.54.3.864. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. 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]
  10. Hartley B. S. Strategy and tactics in protein chemistry. Biochem J. 1970 Oct;119(5):805–822. doi: 10.1042/bj1190805f. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Houmard J., Drapeau G. R. Staphylococcal protease: a proteolytic enzyme specific for glutamoyl bonds. Proc Natl Acad Sci U S A. 1972 Dec;69(12):3506–3509. doi: 10.1073/pnas.69.12.3506. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. 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]
  13. Jaton J. C. Comparison of the amino acid sequences of the variable domains of two homogeneous rabbit antibodies to type III pneumococcal polysaccharide. Biochem J. 1975 May;147(2):235–247. doi: 10.1042/bj1470235. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. 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]
  15. Johnstone A. P., Mole L. E. N-terminal sequences of secretory piece and of alpha chains of different allotype in rabbit secretory IgA. Nature. 1975 Jul 24;256(5515):339–340. doi: 10.1038/256339a0. [DOI] [PubMed] [Google Scholar]
  16. Johnstone A. P., Mole L. E. The subunit and polypeptide-chain structure of rabbit secretory immunoglobulin A. Isolation of a proteolytic fragment suitable for sequence studies on the variable region of alpha-chain. Biochem J. 1977 Oct 1;167(1):245–253. doi: 10.1042/bj1670245. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. KOSTKA V., CARPENTER F. H. INHIBITION OF CHYMOTRYPSIN ACTIVITY IN CRYSTALLINE TRYPSIN PREPARATIONS. J Biol Chem. 1964 Jun;239:1799–1803. [PubMed] [Google Scholar]
  18. Kim B. S., Dray S. Identification and genetic control of allotypic specificities on two variable region subgroups of rabbit immunoglobulin heavy chains. Eur J Immunol. 1972 Dec;2(6):509–514. doi: 10.1002/eji.1830020608. [DOI] [PubMed] [Google Scholar]
  19. Köhler H., Shimizu A., Paul C., Moore V., Putnam F. W. Three variable-gene pools common to IgM, IgG and IgA immunoglobulins. Nature. 1970 Sep 26;227(5265):1318–1320. doi: 10.1038/2271318a0. [DOI] [PubMed] [Google Scholar]
  20. Mole L. E., Jackson S. A., Porter R. R., Wilkinson J. M. Allotypically related sequences in the Fd fragment of rabbit immunoglobulin heavy chains. Biochem J. 1971 Sep;124(2):301–318. doi: 10.1042/bj1240301. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Mole L. E. Structural studies on rabbit immunoglobulin allotypes. Biochem Soc Trans. 1976;4(1):33–34. doi: 10.1042/bst0040033. [DOI] [PubMed] [Google Scholar]
  22. Mole L. R. A genetic marker in the variable region of rabbit immunoglobulin heavy chain. Biochem J. 1975 Nov;151(2):351–359. doi: 10.1042/bj1510351. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. 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]
  24. Offord R. E. Electrophoretic mobilities of peptides on paper and their use in the determination of amide groups. Nature. 1966 Aug 6;211(5049):591–593. doi: 10.1038/211591a0. [DOI] [PubMed] [Google Scholar]
  25. Prahl J. W., Tack B. F., Todd C. W. Rabbit immunoglobulin lacking group a allotypic specificities. 3. Variable region structure and genetic control. Biochemistry. 1973 Dec 4;12(25):5181–5186. doi: 10.1021/bi00749a026. [DOI] [PubMed] [Google Scholar]
  26. 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]
  27. Smithies O., Gibson D., Fanning E. M., Goodfliesh R. M., Gilman J. G., Ballantyne D. L. Quantitative procedures for use with the Edman-Begg sequenator. Partial sequences of two unusual immunoglobulin light chains, Rzf and Sac. Biochemistry. 1971 Dec 21;10(26):4912–4921. doi: 10.1021/bi00802a013. [DOI] [PubMed] [Google Scholar]
  28. Summers M. R., Smythers G. W., Oroszlan S. Thin-layer chromatography of sub-nanomole amounts of phenylthiohydantoin (PTH) amino acids on polyamide sheets. Anal Biochem. 1973 Jun;53(2):624–628. doi: 10.1016/0003-2697(73)90114-0. [DOI] [PubMed] [Google Scholar]
  29. Van Hoegaerden M., Strosberg A. D. Partial amino acid sequence in the N-terminal region of an anti-Micrococcus lysodeikticus antibody heavy chain of allotype a 1. FEBS Lett. 1976 Jul 1;66(1):35–38. doi: 10.1016/0014-5793(76)80579-0. [DOI] [PubMed] [Google Scholar]
  30. 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]
  31. Woods K. R., Wang K. T. Separation of dansyl-amino acids by polyamide layer chromatography. Biochim Biophys Acta. 1967 Feb 21;133(2):369–370. doi: 10.1016/0005-2795(67)90078-5. [DOI] [PubMed] [Google Scholar]

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

RESOURCES