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Interaction of Protein Antigens and Antibodies

I. Inhibition Studies with the Egg Albumin-anti-Egg Albumin System¹

From the Division of Agricultural Biochemistry, University of Minnesota, St. Paul 1, Minn.

Abstract

Studies on the inhibition of the egg albumin-anti-egg albumin reaction have been conducted with 20 amino acids and acetylated amino acids and 40 related compounds to determine the extent and possible specificity of any inhibitory effects. Relatively high concentrations of the amino acids and acetylated amino acids were required to produce inhibition and no specificity of their effects was apparent. Variable inhibitory effects were noted with compounds having different chemical properties. The inhibition produced by substances with similar functional groups appeared to increase with increase in the molecular weight of the compound tested.

The inhibition of precipitate formation by KF, KCl, KBr, KI, and KCNS decreased in the same order as the familiar lyotropic series, CNS^– ; I^– ; Br^– ; Cl^– ; F^–. With these inorganic anions increase in degree of hydration is accompanied by decreased inhibitory power.

The effect of pH on the egg albumin-anti-egg albumin reaction has been measured and interpreted in terms of the groups of the interacting proteins which undergo change in the pH ranges where onset of inhibition is noted.

Footnotes

¹ Supported in part by a research grant from the National Institutes of Health, Public Health Service. Taken from a portion of a thesis submitted by W. J. Kleinschmidt in partial fulfillment of the requirements for the Ph.D. degree. Scientific Journal Series paper No. 2740, Minnesota Agricultural Experiment Station.

² Present address, Lilly Research Laboratories, Indianapolis, Indiana.