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From the Department of Medicine, Harvard Medical School, and The Medical Services, Massachusetts General Hospital, Boston, Massachusetts
Abstract
Human immunoconglutinin was titrated by its reaction with sensitized sheep erythrocytes alexinated with horse complement. IC was shown to be a euglobulin and to be sensitive to the action of 2-mercaptoethanol. On Sephadex G200 chromatography and density gradient ultracentrifugation, its behavior was that of a macroglobulin. IC activity was absorbed by an antiserum to human IgM globulins. In contrast to bovine conglutinin, IC did not require calcium ions for its action, and was not inhibited by N-acetyl-D-glucosamine. Sequential complement fixation at least as far as AgAbC'1423 is required for IC to react with alexinated complexes. Reactivity with autologous complement was demonstrated.
Footnotes
1 This is publication No. 405 of the Robert W. Lovett Memorial Group for the Study of Diseases Causing Deformities, Harvard Medical School, at the Massachusetts General Hospital. It was supported by Grants AM TI 5067 (to J. B.) and AM-3564 from the National Institute of Arthritis and Metabolic Diseases, National Institutes of Health and the Charles A. King Trust of the Massachusetts General Hospital.
2 Senior Investigator, Arthritis Foundation.
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