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The Journal of Immunology, 1972, 108: 289-294.
Copyright © 1972 by The American Association of Immunologists, Inc.

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Immunoglobulin M: Identification of an Unusual Fragment Following High Temperature Trypsin Proteolysis1

Andrew G. Plaut, Nickolas Calvanico and Thomas B. Tomasi, Jr.

Department of Medicine, School of Medicine State University of New York at Buffalo, Buffalo, New York 14814

Abstract

A fragment (Int-L) of m.w. 20,000 containing 25% carbohydrate has been identified in (Fc) preparations obtained from high temperature trypsin digests of human {lambda} type IgM molecules. This fragment consists of two disulfide linked components, one related to {lambda} light chains and the second a portion of µ chain which presumably contains the carbohydrate. The intact fragment is univalent with respect to most anti-{lambda} antisera which precipitate it only following reduction of disulfide bonds.

The Int-L has not been precisely localized in the IgM molecule. Some evidence indicates it may arise from outside the Fab fragment raising the possibility that it represents a third L chain per IgM subunit.

Footnotes

1 This work was supported in part by National Institutes of Health Grant No. 5 RO1 AM 10419 from the United States Public Health Service, and Henry and Bertha Buswell Research Fellowship.




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