PROTEINS FROhi EPIDERMIS 173 4e Figure 1. Agar gel precipitation patterns of the antiserum prepared against the urea antigens verstts urea antigens (D), of the untrcatcd antiserum, and of the antiserum pretreated with 184 txg d (slide I), 440 txg e (slide II), and 360 txg f (slide III) versus alkali antigens (E), of the untreated antiserum, and of thc antiserum pretreated with 184 txg d (slide IV), 88 txg e (slide V), and 360 txg f (slide VI) and versus to•:ofibrin-derived antigens (F), of the untreated antiserum, and of the antiserum pretreated with 184 t•g d (slide VII), 176 txg e (slide VIII), and 180/•g f (slide IX)

174 JOURNAL OF THE SOCIETY OF COSMETIC CHEMISTS Figure 2. Agar gel prccipitation patterns of the antiserum prcparcd against the alkali anti- gens versus the alkali antigens (E), of the untrcatcd antiserum, and of the antiscrum pre- treated with 400/•g d (slide I), 88/•g c (slide II), and 180/•g f (slide III) and versus the tono- fibrin-derived antigens (F), of the tintreated antiscrum, and of the antisorton pretreated with 400/•g d (slide IX'), 88/•g e (slide V), and 180/•g f (slide VI) sera in all cases were first pretreated with 10 td of normal human serum to telhOVe traces of antibodies developed against the serum proteins. In Fig. 4, the antisera 4, 5, and 6 were placed in the center wells and the antigens in duplicate in six wells surrounding the antisera. The urea antigens (D) reacted strongly with the antiserum prepared against the urea proteins. Several bands of precipitation developed and the formation of these bands was inhibited (Fig. 1, slide I) by pretreat- ment of the antiserum with the urea antigens, d. Pretreatment of this antiserum with 440 t•g of the alkali antigens, e, did not completely inhibit precipitin band formation (slide II), while pretreatment of the antiserum with the tonofibrin-derived antigens, f, completely inhibited band forma-