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A Physical-Chemical Study of Normal and Immune Horse Sera

From the Research Laboratories of Parke, Davis and Company, Detroit, The Laboratory of Physiological Chemistry, Yale University, and The Sterling Chemistry Laboratory, Yale University

Abstract

A survey has been made of the electrophoretic and ultracentrifugal behavior of immune horse sera and purified antiserumpreparations produced by immunization with the following antigens: diphtheric, scarlet-fever streptococcal, tetanal and perfringens-toxins and pneumococcal (type 1 and 2) vaccines.

A comparison of the immune sera and plasmas with normal serum and plasma in the electrophoretic apparatus of Tiselius with the aid of the unmodified Toepler schlieren-band analysis shows that, under the experimental conditions employed, no extra proteic component appears in the serum following immunization with any of the toxins mentioned. A roughly quantitative evaluation of the electrophoretic diagrams obtained with the schlieren-scanning method of Longsworth reveals significant increases in the relative concentration of either the - or the -globulin present in immune sera as compared with normal serum or plasma. The diagrams given by the enzymatically purified antitoxins were invariably much less complex than those given by the unfractionated sera and indicated the absence or greatly diminished concentration of albumin and the predominance of globulins of low mobility at pH 8 (- and -globulin).

With the exception of scarlet-fever antitoxin, the electrophoretic fractionation of purified antibody-preparations in the separative apparatus of Tiselius did not lead to significant increases of the specific antitoxic activity in the various fractions obtained. With the exception of antipneumococcic serum the same is true for the experiments in which diluted immune sera were subjected to molecular sedimentation in an air-driven ultracentrifuge designed by Beams; the gravitational fields employed were of the order of 66,000 gr. This result tends to show that the antibody-activity in the preparations examined is not linked to heavy proteic molecules of the type previously found in antipneumococcic horse sera.

Footnotes

¹ Present address—Northern Regional Research Laboratory, U. S. Department of Agriculture, Peoria, Illinois.