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The Journal of Immunology, 1972, 109: 59-64.
Copyright © 1972 by The American Association of Immunologists, Inc.
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Identification of "J" Chain in a Homogeneous Canine IgA Immunoglobulin1

J. Michael Kehoe2, Thomas B. Tomasi, Jr.3, Farielle Ellouz2 and J. Donald Capra2

From the Department of Microbiology, Mount Sinai School of Medicine of the City University of New York, New York, New York and the Department of Medicine, State University of New York, E. J. Meyer Memorial Hospital, Buffalo, New York

Abstract

A homogeneous IgA protein was isolated from the serum of a dog with myelomatous disease. Analytical ultracentrifugation showed that approximately 60% of this protein existed as an 11S component and the remainder as higher order polymers. The reactivity of the intact protein with an anti-human "J" chain antiserum implied that it contained a considerable amount of a "J" component. This was confirmed by the isolation of a highly acidic polypeptide by gel-filtration and ion-exchange chromatography from the 11S IgA after reduction. The amino acid composition of this polypeptide corresponded closely to that reported by others for human "J" components.

Footnotes

1 Supported by National Science Foundation Grant GB-17046, National Institutes of Health Grant AI-09810, and a Grant-in-Aid from the New York Heart Association to J. D. C. and J. M. K. (J. M. K. is an Established Investigator of the American Heart Association; J. D. C. is the recipient of NIH Career Development Award #6K4-GM35, 190-01.)

2 Department of Microbiology, Mount Sinai School of Medicine of The City University of New York, 10 East 102nd Street, New York, New York 10029.

3 Department of Medicine, State University of New York, E. J. Meyer Memorial Hospital, 426 Grider Street, Buffalo, New York 14215.






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