Skip to main content
PMC home page
The Journal of Experimental Medicine logoLink to The Journal of Experimental Medicine
. 1968 May 1;127(5):967–982. doi: 10.1084/jem.127.5.967

THE SUBUNITS IN RABBIT ANTI-FORSSMAN IGM ANTIBODY

Michael M Frank 1, John H Humphrey 1
PMCID: PMC2138488  PMID: 5655105

Abstract

Rabbit IgM anti-Forssman antibody was highly purified and the subunits obtained on reduction and alkylation were labeled radioactively and isolated by two different and unrelated methods. In both cases the subunits were found to have a molecular weight of about 90,000, based on their behavior on density gradient centrifugation and gel filtration, and evidence is given that they contained one light and one heavy chain. The subunits bound only weakly to sheep erythrocyte stroma, and only half could be shown to possess antigen specific sites. The data are consistent with the concept that each anti-Forssman IgM molecule has five effective binding sites, but it is uncertain whether the ineffectiveness of the remaining five H-L chain pairs is inherent in the structure of the IgM molecule or an artifact due to the isolation procedure. Intact IgM anti-Forssman antibody binds very firmly to structures containing multiple repeating antigen sites, and it appears that this is due to the presence of multiple binding sites on the molecule.

Full Text

The Full Text of this article is available as a PDF (843.0 KB).

Selected References

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

  1. BOWMAN W. M., MAYER M. M., RAPP H. J. Kinetic studies on immune hemolysis. II. The reversibility of red cell-antibody combination and the resultant transfer of antibody from cell to cell during hemolysis. J Exp Med. 1951 Aug;94(2):87–110. doi: 10.1084/jem.94.2.87. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. CHARLWOOD P. A. Applications of radioactively labeled marker proteins in density gradient ultracentrifugation. Anal Biochem. 1963 Mar;5:226–245. doi: 10.1016/0003-2697(63)90120-9. [DOI] [PubMed] [Google Scholar]
  3. DEUTSCH H. F., MORTON J. I. Dissociation of human serum macroglobulins. Science. 1957 Mar 29;125(3248):600–601. doi: 10.1126/science.125.3248.600. [DOI] [PubMed] [Google Scholar]
  4. GREENBURY C. L., MOORE D. H., NUNN L. A. THE REACTION WITH RED CELLS OF 7S RABBIT ANTIBODY, ITS SUB-UNITS AND THEIR RECOMBINANTS. Immunology. 1965 Apr;8:420–431. [PMC free article] [PubMed] [Google Scholar]
  5. Hill W. C., Cebra J. J. Horse anti-SI immunoglobulins. I. Properties of gamma-M-antibody. Biochemistry. 1965 Dec;4(12):2575–2584. doi: 10.1021/bi00888a005. [DOI] [PubMed] [Google Scholar]
  6. Kaplan M. E., Kabat E. A. Studies on human antibodies. IV. Purification and properties of anti-A and anti-B obtained by absorption and elution from insoluble blood group substances. J Exp Med. 1966 Jun 1;123(6):1061–1081. doi: 10.1084/jem.123.6.1061. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Kennedy J. C., Till J. E., Siminovitch L., McCulloch E. A. The proliferative capacity of antigen-sensitive precursors of hemolytic plaque-forming cells. J Immunol. 1966 Jun;96(6):973–980. [PubMed] [Google Scholar]
  8. Lamm M. E., Small P. A., Jr Polypeptide chain structure of rabbit immunoglobulins. II. gamma-M-immunoglobulin. Biochemistry. 1966 Jan;5(1):267–276. doi: 10.1021/bi00865a035. [DOI] [PubMed] [Google Scholar]
  9. MILLER F., METZGER H. CHARACTERIZATION OF A HUMAN MACROGLOBULIN. I. THE MOLECULAR WEIGHT OF ITS SUBUNIT. J Biol Chem. 1965 Aug;240:3325–3333. [PubMed] [Google Scholar]
  10. Miller F., Metzger H. Characterization of a human macroglobulin. 3. The products of tryptic digestion. J Biol Chem. 1966 Apr 25;241(8):1732–1740. [PubMed] [Google Scholar]
  11. NOSSAL G. J., SZENBERG A., ADA G. L., AUSTIN C. M. SINGLE CELL STUDIES ON 19S ANTIBODY PRODUCTION. J Exp Med. 1964 Mar 1;119:485–502. doi: 10.1084/jem.119.3.485. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Onoue K., Yagi Y., Grossberg A. L., Pressman D. Number of binding sites of rabbit macroglobulin antibody and its subunits. Immunochemistry. 1965 Dec;2(4):401–415. doi: 10.1016/0019-2791(65)90039-x. [DOI] [PubMed] [Google Scholar]
  13. SCHROHENLOHER R. E., KUNKEL H. G., TOMASI T. B. ACTIVITY OF DISSOCIATED AND REASSOCIATED 19S ANTI-GAMMA-GLOBULINS. J Exp Med. 1964 Dec 1;120:1215–1229. doi: 10.1084/jem.120.6.1215. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Suzuki T., Deutsch H. F. Dissociation, reaggregation, and subunit structure studies of some human gamma-M-globulins. J Biol Chem. 1967 Jun 10;242(11):2725–2738. [PubMed] [Google Scholar]
  15. Suzuki T., Deutsch H. F. Occurrence and properties of a macroglobulin dimer in some hyperglobulinemic sera. J Exp Med. 1966 Nov 1;124(5):819–832. doi: 10.1084/jem.124.5.819. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. TALMAGE D. W., FRETER G. G., TALIAFERRO W. H. The effect of repeated injections of sheep red cells on the hemolytic and combining capacities of rabbit antiserums. J Infect Dis. 1956 May-Jun;98(3):293–299. doi: 10.1093/infdis/98.3.293. [DOI] [PubMed] [Google Scholar]
  17. UTSUMI S., KARUSH F. THE SUBUNITS OF PURIFIED RABBIT ANTIBODY. Biochemistry. 1964 Sep;3:1329–1338. doi: 10.1021/bi00897a024. [DOI] [PubMed] [Google Scholar]

Articles from The Journal of Experimental Medicine are provided here courtesy of The Rockefeller University Press

RESOURCES