Abstract
WE have isolated and identified two intact Cμ4-domain fragments from a monoclonal IgM protein. They differed only in their carbohydrate content, having the same polypeptide chain. They were separated from each other and from Fcμ monomer by molecular exclusion and affinity chromatography (insolubilised concanavalin A1) of mildly reduced and alkylated Fc5μ produced by the method of Plaut and Tomasi2. The Cμ4 fragment containing carbohydrate was designated Cμ4(+) while the carbohydrate-poor domain was called Cμ4(−). These two fragments were identified as Cμ4-domains from their amino acid sequences, amino acid compositions, molecular weights (14,700) and antigenic characteristics. Both fragments originate from tryptic cleavage at Lys-445 of the μ chain (IgM(Ou) numbering3) and could not be further fragmented by extensive reduction and alkylation4. The domain hypothesis of Edelman et al.5 proposes that each homology region of the immunoglobulins evolved to perform independent biological effector functions. Hurst et al.6 have shown that fragmented Cμ4 domain will fix activated Cl(Cl) and will also activate proenzyme Cl to Cl7. Moretta et al.8 have demonstrated receptors specific for IgM on human T lymphocytes, and this has been confirmed by McConnell and Hurd9. We now report that these receptors are specific for the Fc part of IgM (Table 1) and furthermore that the Cμ4 domain is involved in this affinity reaction in a dose-dependent manner (Fig. 1).
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Rent or buy this article
Prices vary by article type
from$1.95
to$39.95
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Conradie, J. D., Volanakis, J. E., and Stroud, R. M., Immunochemistry, 12 967–971 (1975).
Plaut, A. G., and Tomasi, T. B., Proc. natn. Acad. Sci. U.S.A., 65, 318–322 (1970).
Putnam, F. W., Florent, G., Paul, C., Shinoda, T., and Shimizu, A., Science, 182, 287–291 (1973).
Bubb, M. O., and Conradie, J. D., Immun. Commun., (in the press).
Edelman, G. M., et al., Proc. natn. Acad. Sci. U.S.A., 63, 78–85 (1969).
Hurst, M. M., Volanakis, J. E., Hester, R. B., Stroud, R. M., and Bennett, J. C., J. exp. Med., 140, 1117–1121 (1974).
Hurst, M. M., Volanakis, J. E., Stroud, R. M., and Bennett, J. C., J. exp. Med., 142, 1322–1326 (1975).
Moretta, L., Ferrarini, M., Durante, M. L., and Mingari, M. C., Eur. J. Immun., 5, 565–569 (1975).
McConnell, I., and Hurd, C. M., Immunology, 30, 835–839 (1976).
Mayer, M. M., in Experimental Immunochemistry, second ed. (edit. by Kabat, E. A., and Mayer, M. M.), 133 (Thomas, Springfield, Illinois, 1961).
Conradie, J. D., and Visser, L., Immunochemistry, 10, 689–694 (1973).
Williams, C. A., and Chase, M. W. (eds) Methods in Immunology and Immunochemistry first ed., 273 (Academic, New York and London, 1968).
Kehoe, J. M., and Fougereau, M., Nature, 224, 1212–1213 (1969).
Ovary, Z., Saluk, P. H., Quijada, L., and Lamm, M. E., J. Immun., 116 1265–1271 (1976).
Hester, R. B., Mole, J. E., and Schrohenloher, R. E., J. Immun., 114, 486–491 (1975).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
CONRADIE, J., BUBB, M. Cμ4 domain of IgM has cytophilic activity for human lymphocytes. Nature 265, 160–161 (1977). https://doi.org/10.1038/265160a0
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1038/265160a0
This article is cited by
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.