STUDIES ON THE DENATURATION OF ANTIBODY

Author:

Wright George G.1

Affiliation:

1. From the Gates and Crellin Laboratories of Chemistry, California Institute of Technology, Pasadena

Abstract

The specific rate of inactivation of antitoxin in urea solutions, as measured by the Römer neutralization test with toxin, has been shown to be independent of the concentration of protein under the conditions studied. The amount of precipitate obtained in the quantitative precipitation test with toxin, however, increases greatly with increasing protein concentration during denaturation. The time during which the protein concentration is important in this respect has been shown to be the interval in which the urea is being dialyzed from the solutions. The meaning of the results is discussed.

Publisher

Rockefeller University Press

Subject

Immunology,Immunology and Allergy

Cited by 13 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Analysis of solvent-mediated conformational changes of insulin by radioimmunoassay (RIA) techniques;Journal of Pharmaceutical and Biomedical Analysis;1986-01

2. Kinetics of the Formalin Inactivation of Poliovirus;Journal of Medicinal Chemistry;1963-11

3. Some Factors in the Interpretation of Protein Denaturation;Advances in Protein Chemistry;1959

4. The Chemical Nature of Antibodies;Advances in Protein Chemistry Volume 12;1957

5. Die Antigen-Antikörper Bindung;Fortschritte der Serologie;1955

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