Affinity Labelling of Antibodies with Aryl Nitrene as Reactive Group (original) (raw)
- Letter
- Published: 01 November 1969
Nature volume 224, pages 511–512 (1969)Cite this article
- 1727 Accesses
- 232 Citations
- 15 Altmetric
- Metrics details
Abstract
THE covalent binding of a haptene to its specific antibody with a view to identifying the section of peptide chains which form the combining site has been pioneered by Singer _et al._1,2, who named this approach affinity labelling. Antibodies were prepared in rabbits against several aromatic haptenes such as benzene arsonate, and affinity labelling was performed by reaction with _p_-(arsonic acid)-benzene diazonium fluoroborate through the reactive diazonium group. The reaction with specific antibody was considerably more rapid than that with inert IgG because of the concentration of reagent in the combining site. Subsequent separation of heavy and light chains followed by enzymic digestion led to the isolation of one predominant dipeptide (Val-Tyr) from the light chain and another (Thr-Tyr) from the heavy chain; both of these were substituted on the tyrosine residue. No sequence data were available on the peptide chains of rabbit IgG, but from comparison with the known sequences of the light chains of human and mouse IgG it was suggested that the tyrosine residue 86 in the light chain may have been the one labelled.
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
Buy this article
- Purchase on SpringerLink
- Instant access to the full article PDF.
USD 39.95
Prices may be subject to local taxes which are calculated during checkout
Additional access options:
Similar content being viewed by others
References
- Singer, S. J., and Doolittle, R. F., Science, 153, 13 (1966).
Article ADS CAS Google Scholar - Singer, S. J., Slobin, L. I., Thorpe, N. O., and Fenton, J. W., Cold Spring Harbor Symp. Quant. Biol., 23, 99 (1967).
Article Google Scholar - Koyama, J., Grossberg, A. L., and Pressman, D., Biochemistry, 7, 1935 (1968).
Article CAS Google Scholar - Chaimorich, H., Vaughan, R. J., and Westheimer, F. H., J. Amer. Chem. Soc., 90, 4088 (1968).
Article Google Scholar - Eisen, H. N., Methods in Medical Research, 10, 94 (1964).
CAS PubMed Google Scholar - Eisen, H. N., Methods in Medical Research, 10, 106 (1964).
CAS PubMed Google Scholar - Small, P. A., and Lamm, M. E., Biochemistry, 5, 259 (1966).
Article CAS Google Scholar - Givol, D., and Porter, R. R., Biochem. J., 97, 32c (1965).
Article CAS Google Scholar - Fruchter, R. R., Jackson, S. A., Mole, L. E., and Porter, R. R., Biochem. J. (in the press).
Author information
Authors and Affiliations
- Department of Biochemistry, MRC Immuriochemistry Unit,
G. W. J. FLEET & R. R. PORTER - Dyson Perrins Laboratory, University of Oxford,
J. R. KNOWLES
Authors
- G. W. J. FLEET
- R. R. PORTER
- J. R. KNOWLES
Rights and permissions
About this article
Cite this article
FLEET, G., PORTER, R. & KNOWLES, J. Affinity Labelling of Antibodies with Aryl Nitrene as Reactive Group.Nature 224, 511–512 (1969). https://doi.org/10.1038/224511a0
- Received: 03 August 1969
- Issue date: 01 November 1969
- DOI: https://doi.org/10.1038/224511a0
This article is cited by
High-resolution patterning of colloidal quantum dots via non-destructive, light-driven ligand crosslinking
- Jeehye Yang
- Donghyo Hahm
- Moon Sung Kang
Nature Communications (2020)
Photodissociative Cross-Linking of Non-covalent Peptide-Peptide Ion Complexes in the Gas Phase
- Huong T. H. Nguyen
- Prokopis C. Andrikopoulos
- František Tureček
Journal of the American Society for Mass Spectrometry (2018)
Efficient Covalent Bond Formation in Gas-Phase Peptide–Peptide Ion Complexes with the Photoleucine Stapler
- Christopher J. Shaffer
- Prokopis C. Andrikopoulos
- František Tureček
Journal of the American Society for Mass Spectrometry (2016)
Exploring the flexible chemistry of 4-fluoro-3-nitrophenyl azide for biomolecule immobilization and bioconjugation
- Saroj Kumar
- Dileep Kumar
- Pradip Nahar
Analytical and Bioanalytical Chemistry (2016)
Selective chemical protein modification
- Christopher D. Spicer
- Benjamin G. Davis
Nature Communications (2014)