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The Journal of Immunology, 1975, 115: 993-997.
Copyright © 1975 by The American Association of Immunologists, Inc.
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Identification and Properties of J Chain Isolated from Catfish Macroglobulin1

Jiri Mestecky, Rose Kulhavy, Ralph E. Schrohenloher, Milan Tomana and Genesis P. Wright

From the Institute of Dental Research, Departments of Microbiology and Medicine, University of Alabama in Birmingham, Birmingham, Alabama 35294

Abstract

After the cleavage of disulfide bonds of macroglobulin isolated from channel catfish (Ictalurus punctatus), an electrophoretically fast-moving polypeptide, which resembled human J chain, was released. On a Sephadex G-200 column equilibrated in 5 M guanidine, the elution position of the J chain overlapped with the descending part of the L chain peak. Further purification was achieved by DEAE ion-exchange chromatography. The isolated polypeptide, which had a molecular weight of 14,800 ± 500, as determined ultracentrifugally by sedimentation equilibrium in 5 M guanidine, contained 7% carbohydrate with one residue of fucose, two of mannose, one of galactose, two of glucosamine, and one of sialic acid per chain. A comparison of catfish and human J chain amino acid analyses showed the former to have a higher content of serine, glycine, and phenylalanine and a lower content of aspartic acid, isoleucine, and arginine. Tryptic peptide maps of catfish and human J chains revealed very few common peptides. Rabbit and guinea pig antisera to human J chain did not cross-react with catfish J chain. Untreated, resuced and alkylated, S-sulfonated, or cyanogen bromide cleaved macroglobulin from the gar (Lepisosteus osseus) contained no polypeptide analogous to either catfish or human J chain by the criteria employed in this study.

Footnotes

1 This investigation was supported by United States Public Health Service Grants AI-10854, AI-10664, and DE-02670.






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