PROTEINS FROM EPIDERMIS 151 her. Although tono[ibrin-derived proteins have a different source (tono- fibrin) and an isoelectric point (pH 4.5) different from that of the urea and alkali proteins (pH 5.5), their immunodiffusion patterns were quite similar. These complex interrelationships are under further study. Ac- cording to electrophoretic and schlieren patterns (sedimentation) of the urea and alkali proteins of mouse epidermis, normal and pathological (3), and of human epidermis (13), these proteins appeared homogenous. The alkali and urea proteins of mouse epidermis differ significantly in such properties as viscosity increment, axial ratio, frictional coefficient, sedimentation constant, and molecular weight (3) the sedimentation constants of the urea and alkali proteins of human epidermis are also dif- ferent (3). However, these differences in physical properties may be due to varying' sizes of the same proteins extracted by the different reagents. Since the urea proteins (epidermin) of Rudall (1) and tonofibrin of Roe (7, 8) may be involved in keratinization (according to these investigators), further work is necessary to determine the relationships of the alkali and tonofibrin-derived proteins to keratinization. ACKNOWLEDGMENT The skilled assistance of Miss A. Baumler is gratefully acknowledged. (Received August 8, 1969) REFERENCES (1) Rudall, K. M., The proteins of mammalian epidermis, Advan. Proteitz Chem., 7, 253- 90 (1952). (2) Carruthers, C., •,Voernley, D. L., Baumler, A., and Kress, B., Proteins of mammalian epidermis, J. Inve, t. Dermatol., 25, 89-101 (1955). (g) Carrnthers, C., Woernley, D. L., Baumler, A., and Lilga, K., Studies on certain proteins in normal and pathological epidermis, Brit. J. Cattcer, 11, 597-604 (1957). (4) Carruthers, C., Woernley, D. L., Baumler, A., and Shorts, H., The strnctural proteins of epidermis and their possible relation to aging skin, J. Soc. Cosmetic Chemists, 6, 324-43 0955). (5) Crounse, R. G., Epidermal kerrtin: A re-evaluation, Nature, 201), 539-42 (1963). (6) Mercer, E. H., and Olofsson, B., Sedimentation analysis of an extract of tfie prekerati- nous layers of skin, J. Polym, er Sci., 6, 261-9 (1951) . (7) Roe, D. A., A fibrous keratin precursor from the human epidermis. I. The extrac- tion and physical properties of a fibrous protein fmtnd in the human epidermis, I. In- vest. Dermatol., 27, 1-8 (1956). (8) Roe, D. A., Further studies of a fibrous keratin precursor from the human epidermis, Ibid., 27, 319-24 (1956). (9) Rothberg, S., The synthesis of epidermis proteins. I. Alkali solnbilized (insolnble) protein, Ibid., 4•, 151-7 (1964). (10) Rothberg, S., The synthesis of epidermal proteins. II. Solnble proteins, Ibid., 4,% 159- 64 (1964).

182 JOURNAL OF THE SOCIETY OF COSMETIC CHEMISTS (11) Rothbcrg, S., Crounse, R. G., Davis, L., Jr., Awgardo, L., and Lamas, J., The amino acid composition of protein fractions from normal and abnormal epidermis, Ibid., 44, 32O-5 (1965). (12) Woernley, D. L., Carruthers, C., Regent, L., and Baumler, A., The effect of extraction procedures on sedimentation properties of epidermal proteins, Arch. Biochem. Biophys., 66, 167-76 (1957). (13) Carruthers, C., Woernley, D. L., and Baumler, A., Unpublished observations, 1958. SCC Medal Award to Charles Zviak The Society of Cosmetic Chemists has presented its 1969 Medal Award to Mr. Charles Zviak, Vice President Development and Applied Research, L'Oreal, Paris, France. The Society's Medal Award, its highest honor, recognizes Mr. Zviak's outstanding contributions to cosmetic science, cosmetic scientists, and the cosmetic industry during his entire professional career. The Medal was formally presented to Mr. Zviak at a dinner dance in his honor on December 2, 1969, at the Americana Hotel, New York City. Mr. Jacques Corr•ze, Chairman of the Board, I•'Oreal of Paris, U.S., served as eulogist for Mr. Zviak. Le[t to right: the Society's President, Mr. Harry Isacoff Eulogist, Mr. Jacques Corrdze and Medalist Charles Zviak