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The Journal of Immunology, 1973, 111: 1367-1375.
Copyright © 1973 by The American Association of Immunologists, Inc.
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A Light Chain Tyrosyl Sequence in the Antibody Site of a Rabbit Anti-p-Azobenzoate Antibody1

O. A. Roholt, B. Friedenson, G. Radzimski and D. Pressman

Department of Biochemistry Research, Roswell Park Memorial Institute, 2 Buffalo, New York 14203

Abstract

A peptide containing a tyrosyl residue from the active site of a rabbit anti-pazobenzoate antibody preparation (from a single rabbit) was isolated as an iododerivative by means of the paired iodination technique. The sequence of the peptide was found to be Tyr-Thr-Gly-(diiodo)Tyr. It was derived from the light chain and was apparently from a hypervariable region since we have not found the corresponding sequence in published light chain sequences. It is the C-terminal tyrosyl residue of this sequence, -Tyr-Thr-Gly-Tyr-, that is in the site since it is almost completely protected from reaction with iodine if specific hapten is present during the iodination. The iodination of this tyrosyl residue does not destroy the binding activity of the site, but only reduces the hapten binding constant, i.e., from about 106 M-1 to 105 M-1 for p-iodobenzoate. This conclusion is based on an approximation procedure for resolving the hapten-binding curves of the uniodinated antibody and of the antibody iodinated in the absence and in the presence of hapten. It is interesting that the N-terminal tyrosyl residue of the isolated sequence was not iodinated at all; thus it is very near to the site but is not exposed to the iodinating reagent.

Footnotes

1 This work was supported in part by Grant AI-3962 from the National Institute of Allergy and Infectious Diseases.

2 A unit of the New York State Department of Health.






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