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The Journal of Immunology, 1961, 86: 431-439.
Copyright © 1961 by The American Association of Immunologists, Inc.

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Properties of Specifically Purified Kidney Localizing Antikidney Antibody1

Yasuo Yagi and David Pressman

From the Department of Biochemistry Research, Roswell Park Memorial Institute, Buffalo, New York

Abstract

1. Significant amount of material containing 18% of the total nitrogen and 60% of the total phosphorus was solubilized by heating lyophilized sediment of rat kidney homogenate at 60°C at pH 8.
2. The heat extract thus obtained partially neutralized the localizing activity of anti-kidney antibody. Therefore, specifically purified antibody prepared by heat elution of adsorbed antibody on untreated kidney sediment seems to be already neutralized to some extent.
3. Electrophoresis on starch of anti-kidney antibody indicated the {gamma}-globulin nature of localizing antibody. A large portion of the {gamma}-globulin from specifically purified antibody was converted to faster migrating components, probably antigen-antibody complexes, after neutralization with the trypsin digest of kidney sediment. Further evidence for the presence of antigen-antibody complexes in specifically purified antibody was also indicated from the electrophoretic results.
4. Ultracentrifugal studies showed that the localizing antibody is primarily in the light {gamma}-globulin and excluded the possibility that it is significantly present in heavy globulins. The radioiodination and the specific purification by adsorption-elution procedure does not seem to cause any appreciable change in the sedimentation properties of antibody globulin.

Footnotes

These studies were supported in part by a grant from the National Heart Institute (Grant H-2092), U. S. Public Health Service.







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