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The Journal of Immunology, 1971, 107: 782-793.
Copyright © 1971 by The American Association of Immunologists, Inc.
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Isolation and Physico-Chemical Characterization of the "IgM-Like" Immunoglobulin from the Stingray Dasyatis Americana1

William H. Johnston, Jr., Ronald T. Acton2, Peter F. Weinheimer3, William Niedermeier, E. Edward Evans, Emma Shelton4 and J. Claude Bennett5

From the Department of Microbiology and Department of Medicine, Division of Clinical Immunology and Rheumatology, University of Alabama in Birmingham, Birmingham, Alabama 35233, and the National Cancer Institute, National Institutes of Health, Bethesda, Maryland

Abstract

The stingray Dasyatis americana was found to synthesize high molecular weight antibodies against Salmonella typhosa "H" antigen and human A erythrocytes. These antibodies were demonstrated to be macroglobulins with a sedimentation coefficient of 17.1S and a molecular weight of 820,000. Carbohydrate analysis revealed a total content of 9.3% and a composition which was distinctively different from human IgM. Complete reduction and alkylation of the stingray macroglobulin, followed by gel filtration in the presence of guanidine hydrochloride, resulted in separation of the heavy (H) and light (L) polypeptide chains. These chains were found to have molecular weights of 70,000 and 23,000 for the H and L chains, respectively. With the exception of a lower content of the basic amino acids, the amino acid composition of the H and L chains was similar to that reported for human macroglobulin polypeptide chains. The stingray macroglobulin was examined by electron microscopy and displayed a pentameric structure. The data suggest a structural similarity between stingray macroglobulin and mammalian IgM.

Footnotes

1 This investigation was supported by grants from the United States Public Health Service (AI-02693, AI-9153, AM-03555), the National Science Foundation (Grant GB-5983), and the John A. Hartford Foundation.

2 Postdoctoral Research Fellow supported by United States Public Health Service Training Grant 5-TOI-00293. Present address: Division of Biology, California Institute of Technology, Pasadena, California 91109.

3 Postdoctoral Research Fellow supported by United States Public Health Service Research Fellowship 1-FO-2AM42874-01A1.

4 Member of the Biosynthesis Section, Laboratory of Biochemistry, National Cancer Institute, Bethesda, Maryland 20014.

5 Recipient of a Research Career Development Award (K3GMO25-386), to whom reprint requests should be addressed.






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