306 JOURNAL OF THE SOCIETY OF COSMETIC CHEMISTS type should be cleaved so as to make the hair pliable and permit it to as- sume the shape of the curlet. This essentially is the advantage of using a more controllable reducing agent, such as the mercaptan employed in cold waving, rather than the harsh reducing agents such as sodium meta bi- sulfite which cleave SS bonds indiscriminately. Even partial reduction of resistant SS bonds accompanied by parallel chain stoppage or increased lateral chain separation raises the unhappy specter that an isolated partly shielded mercaptan group may be formed within the hair. In the subse- quent oxidation step customarily employed to convert the mercaptan to a disulfide crosslink either of the two following situations may arise: 1. The W--SH group finds itself as an isolated entity incapable of re- linking with any neighboring mercaptan group. Subsequent attack by a strong oxidizing agent will succeed in oxidizing this mercaptan to combined cysteic acid. As a result the hair as a fiber is now intrinsically that much weaker for having lost a formerly resistant disulfide linkage, or 2. The W--SH group might be too isolated to allow for its immediate oxidation. In such a case the remaining more favorably situated ruercap- tan groups are converted to disulfide links and this isolated mercaptan is sealed into the interior of the hair. With the passage of time and the continual kinetic chain slippage and folding, this mercaptan group will find itself within the immediate proximity of a disulfide crosslinkage. At such time the distinct possibility of disulfide-mercaptan interchange arises. Owing to the ease with which this interchange (59) can occur, this isolated mercaptan will be capable of acting as an "internal plasticizer," resulting in a slow exchange of S--S and SH bonds along the protein chain and producing stress relaxation or loss of the permanent wave. This effect is similar to what one observes when thiokol rubber under stress is subjected to mercaptan vapor (60). duVigneaud (61) has suggested that a similar mechanism may be responsible for the progressive gradual inactivation of insulin which occurs on the addition of small amounts of cystine to a solu- tion of this protein. On the basis of the results of our "test tube" experiments we cannot, of course, explain all the subtilities of the hair waving process. What we have tried to show in the last section of this article, however, is how infor- mation obtained from these new studies on disulfide cleavage can be used to explain the over-all chemistry of the hair waving process. We hope that our research may help to rationalize the empirical chemical procedures which are now employed in hair waving and to suggest new and more effec- tive methods for the waving of hair. REFERENCES (1) duVigneaud, V., "A Trail of Research in Sulphur Chemistry and Metabolism," Ithaca, Cornell University Press (1952). (2) Calvin, M., Chem. Eng. News, 31, 1735 (1953). (3) Wald, G., and Brown, P. K., 7- Gert. PhydoL, 35, 797 (1952).
PROGRESS IN THE CHEMISTRY OF DISULFIDES 307 (4) For review, see Neurath, H., Greenstein, J.P., Putnam, F. W., and Erickson, J. O., Chem. Rev., 43, 157 (1944). For review, see Sanger, F., Adv. Protein Chem., 7, 1 (1952). Sch6berl, A., Ann., 111, 507 (1933). Sch6berl, A., Beringer, E., and Harren, F., Ber., 67B, 1545 (1934). Sch6berl, A., Ibid., 70B, 186 (1937). Speakman, J. B., 7. Soc. Dyers Colourists, 52, 335 (1936). Sch6berl, A., and Rambacher, P., Ann., 538, 84 (1939). Shinohara, K., 7- Biol. Chem., 105, 241 (1934) Kharasch, N., Potempa, S., and Wehrmeister,'H., Chem. Rev., 39, 295 (1946). Stoves, J. L., Trans. Faraday Soc., 38, 254 (1942). Kharasch, N., op. cit., 276. Speakman, J. B., Proceed. Swed. Instit. Text. Res., 7, 1 (1948). Alexander, P., Carter, D., and Earland, C., 7. Soc. Dyers Colourists, 67, 23 (195l). Speakman, J. B., and Stoves, J. L., Ibid., 52, 335 (1936). Haurowitz, F., "The Chemistry and Biology of Proteins," New York, Academic Press (1950). Lindley, H., and Phillips, H., Biochem. 7., 39, 17 (1945). Phillips, H., and Cuthbertson, M., Ibid., 39, 7 (1945). Bawn, C. E. H., "The Chemistry of High Polymers," New York, Interscience Publishers (1948). Crawshaw, G. H., and Speakman, J. B., 7. Soc. Dyers Colourists, 70, 81 (1954). Birch, S. F., Cullum, T. V., and Dean, R. A., •'. Inst. Petroleum, 39, 206 (1953). Russell, K. E., and Tobolsky, A. V., 7- Am. Chem. Soc., 76, 395 (1954). Sch6nberg, A., Rupp, E., and Gumlich, W., Ber., 66, 1932 (1933). Clarke, H. T., 7- Biol. Chem., 97, 235 (1932). Karchmer, J. H., and Walker, M. T., Anal Chem., 26, 271 (1954). Hughes, E. D., and Ingold, C. K., Trans. Faraday Soc., 37, 657 (1941). Hinsberg, O., Ber., 43, 901 (1910). Price, C. C., and Zomlefer, J., 7. Am. Chem. $oc., 72, 14 (1950). Hinsberg, O., Ber., 45, 2413 (1912). Tobolsky, A. V., and Baysal, B., 7- Am. Chem. Soc., 75, 1757 (1953). Stockmayer, W. H., Howard, R. O., and Clarke, J. T., Ibid., 75, 1756 (1953). Rogers, M. T., and Campbell, T. W., Ibid., 74, 4742 (1952). Hughes, E. W., private communication received March 20, 1954. Pauling, L., Proc. Natl./Icad. Sci., 35, 495 (1949). Calvin, M., op. tit., 1738. (38) Affleck, J. G., and Dougherty, G., 7- Org. Chem., 15, 865 (1950). (39) Birch, S. F., et al., op. tit., 210. (40) Kimball, G., 7- Chem. Phys., 8, 188 (1940). (41) Rothstein, E., 7- Chem. Sot., 1940, 1550. (42) Cohn, E. J., and Edsall, J. T., "Proteins, Amino Acids and Peptides," New York, Reinhold (1943). (43) Remick, A. E., "Electronic Interpretations of Organic Chemistry," New York, John Wiley and Sons (1950). (44) Fieser, L., Rec. tray. chim. Pays-Bas, 69, 410 (1950). (45) Toennies, G., Lavine, T. F., and Bennett, M., 7- Biol. Chem., 112, 493 (1936). (46) Coghill, R. D., _[bid., 114, 419 (1936). (47) Medes, G., and Floyd, N., Blochem. 7., 36, 259 (1942). (48) Fieser, L., op. tit. (49) Clarke, H. T. (Ed.), "The Chemistry of Penicillin," Princeton, Princeton University Press (1949). (50) Fruton, J. S., and Clarke, H. T., 7. BioL Chem., 106, 667 (1934). (51) Sch6berl, A., Angew. Chem., 53, 227 (1940). (52) Affleck, J. G., and Dougherty, G., op. cit. (53) Sch6berl, A., Ber., 70B, 1186 (1937). (54) Arnold, R., 7- Am. Chem. Sot., 72, 731 (1950). (55) Middlebrook, W. R., and Phillips, H., Biochem. 7., 36, 428 (1942). (56) Reed, R. E., DenBeste, M., and Humoiler, F. L., J. Soc. CosMEtre Cx•EM., 1, 109 (1948). (57) Consden, R., and Gordon, A. H., Biochem. 7., 46, 8 (1950). (58) Benesch, R. E., and Benesch, R., 7. Am. Chem. Sot., 75, 4367 (1953). (59) Rosenthal, N. A., and Oster, G., work in progress. (60) Mochulsky, M., and Tobolsky, A. V., Ind. Eng. Chem., 40, 2155 (1948). (6l) duVigneaud, V., private communication, received May 25, 1954. (5) (6) (7) (8) (9) (lO) (11) (12) (13) (14) i15) (16) (17) (18) (19) (20) (21) (22) (23) (24) (25) (26) (27) (28) (29) (30) (31) (32) (33) (34) (35) (36) (37)
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306 JOURNAL OF THE SOCIETY OF COSMETIC CHEMISTS type should be cleaved so as to make the hair pliable and permit it to as- sume the shape of the curlet. This essentially is the advantage of using a more controllable reducing agent, such as the mercaptan employed in cold waving, rather than the harsh reducing agents such as sodium meta bi- sulfite which cleave SS bonds indiscriminately. Even partial reduction of resistant SS bonds accompanied by parallel chain stoppage or increased lateral chain separation raises the unhappy specter that an isolated partly shielded mercaptan group may be formed within the hair. In the subse- quent oxidation step customarily employed to convert the mercaptan to a disulfide crosslink either of the two following situations may arise: 1. The W--SH group finds itself as an isolated entity incapable of re- linking with any neighboring mercaptan group. Subsequent attack by a strong oxidizing agent will succeed in oxidizing this mercaptan to combined cysteic acid. As a result the hair as a fiber is now intrinsically that much weaker for having lost a formerly resistant disulfide linkage, or 2. The W--SH group might be too isolated to allow for its immediate oxidation. In such a case the remaining more favorably situated ruercap- tan groups are converted to disulfide links and this isolated mercaptan is sealed into the interior of the hair. With the passage of time and the continual kinetic chain slippage and folding, this mercaptan group will find itself within the immediate proximity of a disulfide crosslinkage. At such time the distinct possibility of disulfide-mercaptan interchange arises. Owing to the ease with which this interchange (59) can occur, this isolated mercaptan will be capable of acting as an "internal plasticizer," resulting in a slow exchange of S--S and SH bonds along the protein chain and producing stress relaxation or loss of the permanent wave. This effect is similar to what one observes when thiokol rubber under stress is subjected to mercaptan vapor (60). duVigneaud (61) has suggested that a similar mechanism may be responsible for the progressive gradual inactivation of insulin which occurs on the addition of small amounts of cystine to a solu- tion of this protein. On the basis of the results of our "test tube" experiments we cannot, of course, explain all the subtilities of the hair waving process. What we have tried to show in the last section of this article, however, is how infor- mation obtained from these new studies on disulfide cleavage can be used to explain the over-all chemistry of the hair waving process. We hope that our research may help to rationalize the empirical chemical procedures which are now employed in hair waving and to suggest new and more effec- tive methods for the waving of hair. REFERENCES (1) duVigneaud, V., "A Trail of Research in Sulphur Chemistry and Metabolism," Ithaca, Cornell University Press (1952). (2) Calvin, M., Chem. Eng. News, 31, 1735 (1953). (3) Wald, G., and Brown, P. K., 7- Gert. PhydoL, 35, 797 (1952).
PROGRESS IN THE CHEMISTRY OF DISULFIDES 307 (4) For review, see Neurath, H., Greenstein, J.P., Putnam, F. W., and Erickson, J. O., Chem. Rev., 43, 157 (1944). For review, see Sanger, F., Adv. Protein Chem., 7, 1 (1952). Sch6berl, A., Ann., 111, 507 (1933). Sch6berl, A., Beringer, E., and Harren, F., Ber., 67B, 1545 (1934). Sch6berl, A., Ibid., 70B, 186 (1937). Speakman, J. B., 7. Soc. Dyers Colourists, 52, 335 (1936). Sch6berl, A., and Rambacher, P., Ann., 538, 84 (1939). Shinohara, K., 7- Biol. Chem., 105, 241 (1934) Kharasch, N., Potempa, S., and Wehrmeister,'H., Chem. Rev., 39, 295 (1946). Stoves, J. L., Trans. Faraday Soc., 38, 254 (1942). Kharasch, N., op. cit., 276. Speakman, J. B., Proceed. Swed. Instit. Text. Res., 7, 1 (1948). Alexander, P., Carter, D., and Earland, C., 7. Soc. Dyers Colourists, 67, 23 (195l). Speakman, J. B., and Stoves, J. L., Ibid., 52, 335 (1936). Haurowitz, F., "The Chemistry and Biology of Proteins," New York, Academic Press (1950). Lindley, H., and Phillips, H., Biochem. 7., 39, 17 (1945). Phillips, H., and Cuthbertson, M., Ibid., 39, 7 (1945). Bawn, C. E. H., "The Chemistry of High Polymers," New York, Interscience Publishers (1948). Crawshaw, G. H., and Speakman, J. B., 7. Soc. Dyers Colourists, 70, 81 (1954). Birch, S. F., Cullum, T. V., and Dean, R. A., •'. Inst. Petroleum, 39, 206 (1953). Russell, K. E., and Tobolsky, A. V., 7- Am. Chem. Soc., 76, 395 (1954). Sch6nberg, A., Rupp, E., and Gumlich, W., Ber., 66, 1932 (1933). Clarke, H. T., 7- Biol. Chem., 97, 235 (1932). Karchmer, J. H., and Walker, M. T., Anal Chem., 26, 271 (1954). Hughes, E. D., and Ingold, C. K., Trans. Faraday Soc., 37, 657 (1941). Hinsberg, O., Ber., 43, 901 (1910). Price, C. C., and Zomlefer, J., 7. Am. Chem. $oc., 72, 14 (1950). Hinsberg, O., Ber., 45, 2413 (1912). Tobolsky, A. V., and Baysal, B., 7- Am. Chem. Soc., 75, 1757 (1953). Stockmayer, W. H., Howard, R. O., and Clarke, J. T., Ibid., 75, 1756 (1953). Rogers, M. T., and Campbell, T. W., Ibid., 74, 4742 (1952). Hughes, E. W., private communication received March 20, 1954. Pauling, L., Proc. Natl./Icad. Sci., 35, 495 (1949). Calvin, M., op. tit., 1738. (38) Affleck, J. G., and Dougherty, G., 7- Org. Chem., 15, 865 (1950). (39) Birch, S. F., et al., op. tit., 210. (40) Kimball, G., 7- Chem. Phys., 8, 188 (1940). (41) Rothstein, E., 7- Chem. Sot., 1940, 1550. (42) Cohn, E. J., and Edsall, J. T., "Proteins, Amino Acids and Peptides," New York, Reinhold (1943). (43) Remick, A. E., "Electronic Interpretations of Organic Chemistry," New York, John Wiley and Sons (1950). (44) Fieser, L., Rec. tray. chim. Pays-Bas, 69, 410 (1950). (45) Toennies, G., Lavine, T. F., and Bennett, M., 7- Biol. Chem., 112, 493 (1936). (46) Coghill, R. D., _[bid., 114, 419 (1936). (47) Medes, G., and Floyd, N., Blochem. 7., 36, 259 (1942). (48) Fieser, L., op. tit. (49) Clarke, H. T. (Ed.), "The Chemistry of Penicillin," Princeton, Princeton University Press (1949). (50) Fruton, J. S., and Clarke, H. T., 7. BioL Chem., 106, 667 (1934). (51) Sch6berl, A., Angew. Chem., 53, 227 (1940). (52) Affleck, J. G., and Dougherty, G., op. cit. (53) Sch6berl, A., Ber., 70B, 1186 (1937). (54) Arnold, R., 7- Am. Chem. Sot., 72, 731 (1950). (55) Middlebrook, W. R., and Phillips, H., Biochem. 7., 36, 428 (1942). (56) Reed, R. E., DenBeste, M., and Humoiler, F. L., J. Soc. CosMEtre Cx•EM., 1, 109 (1948). (57) Consden, R., and Gordon, A. H., Biochem. 7., 46, 8 (1950). (58) Benesch, R. E., and Benesch, R., 7. Am. Chem. Sot., 75, 4367 (1953). (59) Rosenthal, N. A., and Oster, G., work in progress. (60) Mochulsky, M., and Tobolsky, A. V., Ind. Eng. Chem., 40, 2155 (1948). (6l) duVigneaud, V., private communication, received May 25, 1954. (5) (6) (7) (8) (9) (lO) (11) (12) (13) (14) i15) (16) (17) (18) (19) (20) (21) (22) (23) (24) (25) (26) (27) (28) (29) (30) (31) (32) (33) (34) (35) (36) (37)

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