Hostname: page-component-78c5997874-4rdpn Total loading time: 0 Render date: 2024-11-07T23:30:25.995Z Has data issue: false hasContentIssue false

The Characterization of Anti-lymphocytic Antibodies*

Published online by Cambridge University Press:  11 June 2012

Keith James
Affiliation:
Department of Surgical Science, University of Edinburgh
Get access

Extract

During recent years the heterogeneity of equine antibodies to a variety of antigens has been convincingly demonstrated (Rockey, Klinman and Karush 1964; Raynaud, Iscaki and Mangalo 1965; Allen, Sirisina and Vaughan 1965; Klinman et al. 1966; Klinman and Karush 1967; Johnson and Allen 1968). For example, extensive studies on equine anti-hapten antibodies have shown that the IgG fraction of horse serum contains at least four different proteins, namely the IgGa, IgGb, IgGc and IOS IgG globulins in addition to the IgG(T) and IgM proteins (Rockey et al. 1964; Klinman et al. 1966). These antibodies differ widely in their ability to precipitate the protein-bound hapten and to fix complement, and their concentrations and binding affinities vary considerably during a course of immunization (Klinman et al. 1966).

Type
Research Article
Copyright
Copyright © Royal Society of Edinburgh 1969

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

Footnotes

*

This paper was assisted in publication by a grant from the Carnegie Trust for the Universities of Scotland.

References

References To Literature

Allen, P. Z., Sirisina, S., and Vaughan, J. H., 1965. J. Immunol., 95, 918.CrossRefGoogle Scholar
Clunie, G. J. A., Nolan, B., James, K., Watt, J. G., and Woodruff, M. F. A., 1968. Transplantation, 6, 459.CrossRefGoogle Scholar
James, K., 1969. Prog. Surg., 7, 140.CrossRefGoogle Scholar
James, K., James, Valerie S., Pullar, Diane M., Wood, A., and Logan, E., 1969. [In press.]Google Scholar
Johnston, S. L., and Allen, P. Z., 1968. J. Immunol., 1, 955.CrossRefGoogle Scholar
Jooste, S. V., Lance, E. M., Levey, R. H., Medawar, P. B., Ruskiewicz, M., Sharman, R., and Taub, R. N., 1968. Immunology, 15, 1697.Google Scholar
Klinman, N. R., Rockey, J. H., Frauenberger, G., and Karush, F., 1966 J. Immunol., 96, 587.CrossRefGoogle Scholar
Klinman, N. R., and Karush, F., 1967. Immunochemistry, 4, 387.CrossRefGoogle Scholar
Levey, R. H., and Medawar, P. B., 1966. Proc. Natn. Acad. Sci. U.S.A., 56, 1130.CrossRefGoogle Scholar
Lowry, O. H., Rosebrough, N. J., Farr, L., and Randall, R. J., 1951. J. Biol. Chem., 193, 265.CrossRefGoogle Scholar
Raynaud, M., Iscaki, S., and Mangalo, R., 1965. Annls Inst. Pasteur, Paris, 109, 525.Google Scholar
Riethmüller, G., Riethmüller, D., Stein, H., and Hausen, P., 1968. J. Immunol., 100, 969.CrossRefGoogle Scholar
Rockey, J. H., Klinman, N. R., and Karush, F., 1964. J. Exp. Med., 120, 589.CrossRefGoogle Scholar
Woodruff, M. F. A., 1968. Nature, Lond., 217, 821.CrossRefGoogle Scholar
Woodruff, M. F. A., Reid, B. L., and James, K., 1967. Nature, Lond., 215, 591.CrossRefGoogle Scholar