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The Journal of Immunology, 1962, 89: 336-343.
Copyright © 1962 by The American Association of Immunologists, Inc.

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The Role of Aggregated {gamma}-Globulins in the Anticomplementary Activity of Human and Animal Sera1

Laurence H. Frommhagen and Hugh Fudenberg

From the Viral and Rickettsial Disease Laboratory, California State Department of Public Health, Berkeley, and the Department of Medicine, University of California School of Medicine, San Francisco

Abstract

The formation of anticomplementary aggregates which occur when 7 S {gamma}-globulin is heated is suppressed by the presence of albumin or of {alpha}- or beta-globulins. However, these non-{gamma}-globulin serum protein fractions will not prevent the further aggregation of 9.5 S to 1000 S {gamma}-globulin materials to precipitated components devoid of anticomplementary activity. Hence anticomple-mentary activity cannot be induced in whole serum by heating, and if present in normal "convalescent" whole serum can be abolished by heating the serum at 60 to 65°C. Experiments utilizing heated and nonheated preparations of purified macro-{gamma}-globulin (19 S) and purified nonaggregated 9.5 S {gamma}1A-globulin indicated that molecular size per se is not responsible for the anticomplementary activity of aggregates and further suggested that such activity is restricted to the 7 S component of the three immunoglobulins.

Footnotes

1 This study was supported by Grants E-1475 and H-5997 from the National Institutes of Health, United States Public Health Service and by funds from the Arthritis and Rheumatism Foundation (Northern California Division) and from the Committee on Research, University of California School of Medicine, San Francisco.




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H. H. Fudenberg, R. Hong, and A. Nisonoff
Lattice Formation in Complement Fixation: Studies with Univalent Rabbit Antibody
Science, April 2, 1965; 148(3666): 91 - 93.
[Abstract] [PDF]




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