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. 1977 Oct 1;167(1):245–253. doi: 10.1042/bj1670245

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.

A P Johnstone, L E Mole
PMCID: PMC1183642  PMID: 412497

Abstract

A method was developed for the preparation of a proteolytic fragment of rabbit secretory immunoglobulin A (sIgA) which contains the variable region of the alpha-chain; this fragment is suitable for primary-sequence studies. The serologically defined subclasses of sIgA are shown to correlate partially with the nature of the binding of a constituent chain of sIgA, called secretory piece. Data are also presented on the relative resistance of sIgA to enzymic and reductive cleavage, compared with immunoglobulin G.

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Selected References

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  1. Brownstone A. D. A versatile system for preparative electrophoresis in acrylamide gel. Anal Biochem. 1969 Jan;27(1):25–46. doi: 10.1016/0003-2697(69)90216-4. [DOI] [PubMed] [Google Scholar]
  2. Cebra J. J., Robbins J. B. Gamma-A-immunoglobulin from rabbit colostrum. J Immunol. 1966 Jul;97(1):12–24. [PubMed] [Google Scholar]
  3. Cebra J. J., Small P. A., Jr Polypeptide chain structure of rabbit immunoglobulins. 3. Secretory gamma-A-immunoglobulin from colostrum. Biochemistry. 1967 Feb;6(2):503–512. doi: 10.1021/bi00854a019. [DOI] [PubMed] [Google Scholar]
  4. Cuatrecasas P. Protein purification by affinity chromatography. Derivatizations of agarose and polyacrylamide beads. J Biol Chem. 1970 Jun;245(12):3059–3065. [PubMed] [Google Scholar]
  5. 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]
  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. FLEISCHMAN J. B., PORTER R. R., PRESS E. M. THE ARRANGEMENT OF THE PEPTIDE CHAINS IN GAMMA-GLOBULIN. Biochem J. 1963 Aug;88:220–228. doi: 10.1042/bj0880220. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Fairbanks G., Steck T. L., Wallach D. F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971 Jun 22;10(13):2606–2617. doi: 10.1021/bi00789a030. [DOI] [PubMed] [Google Scholar]
  9. Frangione B. Correlation of the c-terminal sequence of rabbit light chains with allotypes. FEBS Lett. 1969 Jun;3(5):341–342. doi: 10.1016/0014-5793(69)80173-0. [DOI] [PubMed] [Google Scholar]
  10. Gordon A. H., Louis L. N. Preparative acrylamide electrophoresis: a single gel system. Anal Biochem. 1967 Nov;21(2):190–200. doi: 10.1016/0003-2697(67)90180-7. [DOI] [PubMed] [Google Scholar]
  11. Haber E., Stone M. Extensive degradation of antibody by pepsin. Biochemistry. 1967 Jul;6(7):1974–1980. doi: 10.1021/bi00859a014. [DOI] [PubMed] [Google Scholar]
  12. Halpern M. S., Koshland M. E. Noval subunit in secretory IgA. Nature. 1970 Dec 26;228(5278):1276–1278. doi: 10.1038/2281276a0. [DOI] [PubMed] [Google Scholar]
  13. Hanly W. C., Lichter E. A., Dray S., Knight K. L. Rabbit immunoglobulin A allotypic specificities. Localization to two papain fragments, fab 2 and fc 2 , of secretory immunoglobulin A. Biochemistry. 1973 Feb;12(4):733–741. doi: 10.1021/bi00728a025. [DOI] [PubMed] [Google Scholar]
  14. 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]
  15. Johnstone A. P., Mole L. E. Sequence studies on the heavy chain of rabbit immunoglobulin A of different alpha-locus allotypes. Biochem J. 1977 Oct 1;167(1):255–267. doi: 10.1042/bj1670255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Kelus A. S., Gell P. G. Immunoglobulin allotypes of experimental animals. Prog Allergy. 1967;11:141–184. [PubMed] [Google Scholar]
  17. 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]
  18. Knight K. L., Lichter E. A., Hanly W. C. Papain cleavage of rabbit secretory immunoglobulins A. Differential sensitivity of f and g subclasses. Biochemistry. 1973 Aug 14;12(17):3197–3203. [PubMed] [Google Scholar]
  19. Knight K. L., Vetter M. L., Malek T. R. Distribution of covalently bound and non-covalently bound secretory component on sbuclasses of rabbit secretory IgA. J Immunol. 1975 Aug;115(2):595–598. [PubMed] [Google Scholar]
  20. Koshland M. E. Structure and function of the J chain. Adv Immunol. 1975;20:41–69. doi: 10.1016/s0065-2776(08)60206-0. [DOI] [PubMed] [Google Scholar]
  21. Lamm M. E., Greenberg J. Human secretory component. Comparison of the form occurring in exocrine immunoglobulin A to the free form. Biochemistry. 1972 Jul 18;11(15):2744–2750. doi: 10.1021/bi00765a002. [DOI] [PubMed] [Google Scholar]
  22. Lawton A. R., Asofsky R., Mage R. G. Synthesis of secretory IgA in the rabbit. 3. Interaction of colostral IgA fragments with T chain. J Immunol. 1970 Feb;104(2):397–408. [PubMed] [Google Scholar]
  23. 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]
  24. 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]
  25. NISONOFF A., DIXON D. J. EVIDENCE FOR LINKAGE OF UNIVALENT FRAGMENTS OR HALF-MOLECULES OF RABBIT GAMMA-GLOBULIN BY THE SAME DISULFIDE BOND. Biochemistry. 1964 Sep;3:1338–1342. doi: 10.1021/bi00897a025. [DOI] [PubMed] [Google Scholar]
  26. O'Daly J. A., Cebra J. J. Chemical and physicochemical studies of the component polypeptide chains of rabbit secretory immunoglobulin A. Biochemistry. 1971 Oct 12;10(21):3843–3850. doi: 10.1021/bi00797a007. [DOI] [PubMed] [Google Scholar]
  27. O'Daly J. A., Cebra J. J. Rabbit secretory IgA. I. Isolation of secretory component after selective dissociation of the immunoglobulin. J Immunol. 1971 Aug;107(2):436–448. [PubMed] [Google Scholar]
  28. 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]
  29. OUDIN J. [Allotypes of certain serum protein antigens. Immuno-chemical and genetic relationships between 6 principal allotypes observed in rabbit serum]. C R Hebd Seances Acad Sci. 1960 Jan 25;250:770–772. [PubMed] [Google Scholar]
  30. 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]
  31. 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]
  32. STEERS E., Jr, CRAVEN G. R., ANFINSEN C. B., BETHUNE J. L. EVIDENCE FOR NONIDENTICAL CHAINS IN THE BETA-GALACTOSIDASE OF ESCHERICHIA COLI K12. J Biol Chem. 1965 Jun;240:2478–2484. [PubMed] [Google Scholar]
  33. Steward M. W. Resistance of rabbit secretory IgA to proteolysis. Biochim Biophys Acta. 1971 May 25;236(2):440–449. doi: 10.1016/0005-2795(71)90224-8. [DOI] [PubMed] [Google Scholar]
  34. 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]
  35. Tomasi T. B., Grey H. M. Structure and function of immunoglobulin A. Prog Allergy. 1972;16:81–213. [PubMed] [Google Scholar]
  36. Wilkinson J. M. Alpha-chains of immunoglobulin A from rabbits of different allotype: composition and N-terminal sequence. Nature. 1969 Aug 9;223(5206):616–617. doi: 10.1038/223616a0. [DOI] [PubMed] [Google Scholar]
  37. 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]
  38. Zikan J., Mestecky J., Schrohenloher R. E., Tomana M., Kulhavy R. Studies on human secretory immunoglobulin A. V. Trypsin hydrolysis at elevated temperatures. Immunochemistry. 1972 Dec;9(12):1185–1193. doi: 10.1016/0019-2791(72)90292-3. [DOI] [PubMed] [Google Scholar]

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