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The Effect of Enzymic Digestion Upon the Antigenic Properties of Antitoxic and Normal Horse Plasmas

From the Department of Bacteriology, University of Kentucky, Lexington, Ky.

Abstract

The action of the enzymes, Aspergillus oryzae diastase, malt-diastase, and pepsin on antitoxic and normal horse plasmas has been studied. All three enzymes have been found to purify antitoxic plasmas and also to render the antitoxic molecule resistant to subsequent heat-treatment. Evidence has been presented that the antitoxic molecule decreases in size as purification proceeds, and it is suggested that the process of purification of antitoxins by the enzymes studied is essentially a proteolytic one. Normal plasmas appear to be much less resistant to enzymic action than are antitoxic plasmas.

Antigenic studies of the digested products by means of the Schultz-Dale technic have revealed that the digested antitoxins are antigenically closely allied, regardless of which of the three enzymes is used for digestion.

Animals sensitized to undigested normal or undigested antitoxic plasmas do not react to digested antitoxic nor to digested normal plasmas. Animals sensitized to unheated digested plasmas react not only to the homologous antigens but also to undigested plasma. Animals sensitized to digested antitoxic plasmas react to both digested antitoxic and digested normal plasmas, whereas animals sensitized to digested normal plasmas do not react to digested antitoxic plasmas. Heat-treatment affects the antigenic character of the digested antitoxins. Animals sensitized to heat-treated antitoxin fail to react to digested, unheated antitoxin, but do react to undigested, unheated normal or antitoxic serum protein, and also to digested, heated antitoxin.