HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Mole, L. E. Articles by Koshland, M. E. Search for Related Content PubMed Articles by Mole, L. E. Articles by Koshland, M. E.

The Isolation and Characterization of the V_H Domain from Rabbit Heavy Chains of Different a Locus Allotype¹

From the Medical Research Council Immunochemistry Unit, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX13OU, England, and The Department of Bacteriology and Immunology, University of California, Berkeley, California 94720

Abstract

The Fd fragment of rabbit -chains was split by papain to yield a smaller fragment with a molecular weight of approximately 14,000 and dialyzable small peptides and amino acids. The domain size fragment was identified as intact variable region from its amino acid content, its blocked amino-terminus, and two characteristic cysteine-containing peptides, while the small peptides and amino acids were accounted for by the degradation of the C_H1 region. The variable regions isolated from Aa1 and Aa3 Fd fragments not only reacted quantitatively with immunoadsorbents conjugated with the homologous anti-a allotype antibody, but also completely inhibited the binding of the parent Fd fragment to the homologous antibody as measured by radioimmune assay. These data provide direct evidence that the group a allotypic determinants are contained entirely in the variable portion and are independent of the constant portion of rabbit heavy chains.

Footnotes

¹ This work is supported by Research Grant AI 07079 from the National Institute of Allergy and Infectious Diseases, United States Public Health Service.

² Predoctoral trainee of the National Institutes of Health, United States Public Health Service, supported by Grant AI 120.

³ Please address correspondence and requests for reprints to Dr. Marian E. Koshland, Department of Bacteriology and Immunology, University of California, Berkeley, California 94720.

This article has been cited by other articles:

				P. F. Maness, H. Engeser, M. E. Greenberg, M. O'Farrell, W. E. Gall, and G. M. Edelman Activities of the src-gene Product of Avian Sarcoma Virus Cold Spring Harb Symp Quant Biol, January 1, 1980; 44(0): 949 - 958. [Abstract] [PDF]

				D. Givol, J. Sharon, J. Hochman, M. Gavish, D. Inbar, I. Pecht, I.-Z. Steinberg, and J. Schlessinger Folding, Association, and Interactions of Domains in the Antibody Molecule Cold Spring Harb Symp Quant Biol, January 1, 1977; 41(0): 667 - 675. [Abstract] [PDF]

				B. A. Fraser, A. P. Johnstone, S. M. Gordon, and T. J. Kindt The Response of Rabbits to Streptococcal Hyperimmunization Cold Spring Harb Symp Quant Biol, January 1, 1977; 41(0): 689 - 698. [Abstract] [PDF]

				J. D. Capra, D. G. Klapper, A. S. Tung, and A. Nisonoff Identical Hypervariable Regions in Light Chains of Differing V{kappa} Subgroups Cold Spring Harb Symp Quant Biol, January 1, 1977; 41(0): 847 - 853. [Abstract] [PDF]