Welcome to the new version of CaltechAUTHORS. Login is currently restricted to library staff. If you notice any issues, please email coda@library.caltech.edu
Published January 1, 2018 | public
Journal Article

Pillars Article: Evidence for Amino Acid Sequence Differences among Proteins Resembling the L-chain Subunits of Immunoglobulins. J. Mol. Biol. 1965. 12: 81–87


In this study immunoglobulin structural variation was examined through analysis of L-chain type proteins produced by a variety of distinct plasma cell tumors of the mouse. These proteins were examined by serological techniques, quantitative amino acid analysis and peptide mapping. It appeared from these studies that these proteins all contained a common amino acid sequence throughout a large portion of the molecule. Nevertheless, ea.ch of the proteins contained a unique region of amino acid sequence which allowed it to be distinguished from any other on the basis of certain variable peptides. This immediately suggested the possibility of a second chain, loosely linked by non-covalent bonding or joined through disulfide bonding. To examine this possibility, performic acid oxidation and disulfide reduction procedures were carried out. Following these react ions, several methods of separation failed to demonstrate any alteration in either the peptide map patterns or the amino acid composition of these proteins. It seems, therefore, that if a second chain is present it is covalently linked through some bond other than a disulfide bond. It is apparent from 'the peptide map data that variation must occur in some type of "specialized area". Although the role of the various chains of immune globulins is not yet clear, we believe that this remarkable type of amino acid sequence variation reflects in part the mechanism by which specificity is conferred.

Additional Information

© 2018 American Association of Immunologists. Reprinted from Journal of Molecular Biology, Vol. 12, J. C. Bennett, L. E. Hood, W. J. Dreyer, and M. Potter, Evidence for amino acid sequence differences among proteins resembling the L-chain subunits of immunoglobulins, 81–87, Copyright 1965, with permission from Elsevier. We thank Mr John Raes for his excellent technical assistance during the course of this work, which was supported in part by a Public Health Service Research Grant (GMO-6965) and by a Public Health Postdoctoral Fellowship (I-F2-GM-20, 388-01) (LH).

Additional details

August 19, 2023
October 18, 2023