Studies of Cryoproteins in Systemic Lupus Erythematosus

Lonnie B. Hanauer; Charles L. Christian

doi:10.1172/JCI105541

Department of Medicine, Columbia University College of Physicians & Surgeons, and the Edward Daniels Faulkner Arthritis Clinic of the Presbyterian Hospital, New York, N. Y.

†

Postdoctoral trainee, U. S. Public Health Service.

‡

Recipient of investigatorship of the Health Research Council of the City of New York under contract I-178.

Address requests for reprints to Dr. Charles L. Christian, 630 West 168th St., New York, N. Y. 10032.

Submitted for publication August 4, 1966; accepted November 18, 1966.

Supported in part by U. S. Public Health Service research grant AM 04866 from the National Institute of Arthritis and Metabolic Diseases and a grant from the Hartford Foundation.

Find articles by Hanauer, L. in: JCI | PubMed | Google Scholar

Department of Medicine, Columbia University College of Physicians & Surgeons, and the Edward Daniels Faulkner Arthritis Clinic of the Presbyterian Hospital, New York, N. Y.

†

Postdoctoral trainee, U. S. Public Health Service.

‡

Recipient of investigatorship of the Health Research Council of the City of New York under contract I-178.

Address requests for reprints to Dr. Charles L. Christian, 630 West 168th St., New York, N. Y. 10032.

Submitted for publication August 4, 1966; accepted November 18, 1966.

Supported in part by U. S. Public Health Service research grant AM 04866 from the National Institute of Arthritis and Metabolic Diseases and a grant from the Hartford Foundation.

Find articles by Christian, C. in: JCI | PubMed | Google Scholar

Published March 1, 1967 - More info

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Abstract

Cryoproteins observed in patients with systemic lupus erythematosus were shown to be of “mixed type,” consisting largely of IgG and IgM. The IgM moiety possessed anti-IgG globulin reactivity and precipitated in the cold after mixing with a source of IgG. The IgM fraction of one cryoprotein precipitated only with the same patient's IgG. Antisera prepared against purified cryoproteins regularly recognized IgM, IgG, the 11 S component of C′, and α₂-macroglobulin. C′4 (β_1E) and C′3 (β_1C) were recognized by four and two antisera, respectively. Antisera prepared against two cryoproteins reacted (after absorption) only with the sera of origin. These “unique” antigens were associated with IgM, were destroyed by mercaptoethanol treatment, and, in one patient, were shown to disappear subsequent to clinical improvement.

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