TRANSGLUTAMINASE 2 5 removal of the F-layer (45) and incubation with the enzyme. However, this procedure would likely have only academic importance, unless consumer habits, weathering, or normal chemical processing were found to similarly destroy or disrupt the F-layer. Transglutaminase remains an interesting enzyme for investigation of personal care prod- uct applications. Its enzymology is well understood, and an inexpensive bacterially expressed industrial source has recently become available (48). One possible personal care application might be a hair conditioning treatment that did not require hair to donate endogenous residues to the reaction, as in the present case. The enzyme could be used to cross-link soluble protein or modified protein films co-deposited on hair. In this strategy the enzyme would cross-link itself into the protein film, as it does in food product applications (49,50), and remain on the hair. Observable effects on hair might include semipermanent shine enhancement, damage alleviation, or hydration control. The minimum course of action would probably require little or no engineering of the protein film components. Finally, as stated previously, covalent attachment of solution- phase amine donors and multisite bridging might still be possible on hair where the proposed F-layer was removed or damaged through normal processes. However, the effects of these processes on the proposed F-layer would first have to be determined. ACKNOWLEDGMENTS The authors thank M. Busse and R. Zuwala for assistance in sample preparation, R. Solberg for supplying the child's hair, Dr. Martin Griffin, University of Nottingham, UK, for supplying our initial stock of the enzyme, and J. Kissel, B. Kisting, V. T.- L6pez, and D. Moyer, for donating hair. REFERENCES (1) (2) (3) (4) (5) (6) (7) (8) (9) (10) (11) (12) (13) (14) C. R. Robbins, Chemical and Physical Behavior of Human Hair (Springer-Verlag, New York, 1988), pp. 8-13. Z. K. Draelos, Hair cosmetics, Derm. Clin., 9, 19-27 (1991). J. A. Swift and A. C. Brown, The critical determination of fine changes in the surface architecture of human hair due to cosmetic treatment, J. Soc. Cosmet. Chem., 23, 695-702 (1972). E. Tolgyesi, Weathering of hair, Cosmet. Toiletr., 98, 29-33 (1983). V. N. E. Robinson, A study of damaged hair, J. Soc. Cosmet. Chem., 27, 155-161 (1976). J. A. Swift, Fine details on the surface of human hair, Int. J. Cosmet. Sci., 13, 143-159 (1991). Private communication, H.-D. Weigmann, Textile Research Institute, December 1992. K. Yahagi, Silicones as conditioning agents in shampoos, Comun. Jorn, Com. Esp. Deterg., 23, 181- 193 (1992). E. D. Goddard, J. A. Faucher, R.J. Scott, and M. E. Turney, Adsorption of polymer JR on keratinous surfaces--Part II, J. Soc. Cosmet. Chem. 26, 539-550 (1975). R. Y. Lockhead, Conditioning shampoos, Soap Cosmetics/Chem. Spec., 42-49 (October 1992). A. K. Puri and R. T. Jones, An approach to permanent hair conditioning, Proc. of the 14th IFSCC Congress, 2, 1153-1175 (1986). S. Naito and K. Ooshima, Sorption of keratin hydrolyzate to hair and the cosmetic effect, Proc. of the 14th IFSCC Congress, 2, 1177-1193 (1986). N. Lambert and R. B. Freedman, Structural properties of homogeneous protein disulphide-isomerase from bovine liver purified by a rapid high yielding procedure, BiochemJ., 213, 225-234 (1983). University of Reading of Whiteknights House, U.S. Patent 4,853,315 (1989).
26 JOURNAL OF THE SOCIETY OF COSMETIC CHEMISTS (15) J. A. Swift and B. Bews, The chemistry of human hair cuticle. II. The isolation and amino acid analysis of the cell membranes and A-layer, J. Soc. Cosmet. Chem., 25, 355-366 (1974). (16) E. S. Cooperman and V. L. Johnsen, Penetration of protein hydrolysates into human hair strands, Cosmet. Perfum., 88, 19-22 (1973). (17) L. Lorand and P. Stenburg, "Endo-•/-Glutamine: e-Lysine Transferases: Enzymes Which Cross-Link Proteins," in Handbook of Biochemistry and Molecular Biology, Proteins, Vol. 2, G.D. Fasman Ed. (CRC Press, Cleveland, 1976), pp. 669-684. (18) L. Lorand, Fibrinoligase: The fibrin-stabilizing factor system of blood plasma, Ann. N.Y. Acad. Sci., 202, 6-30 (1972). (19) R. B. Credo, C. G. Curtis, and L. Lorand, Ca2+-related regulatory function offibrinogen, Proc. Natl. Acad. Sci. USA, 75, 4234-4237 (1978). (20) P. J. A. Davies, D. R. Davies, A. Levitzki, F. R. Maxfield, P. Milhaud, M. C. Willingham, and I. H. Pastan, Transglutaminase is essential in receptor-mediated endocytosis of ot2-macroglobulin and polypeptide hormones, Nature, 283, 162-167 (1980). (21) H. G. Williams-Ashman, A. C. Natides, S.S. Pabalan, and L. Lorand, Transamidase reactions involved in the enzymic coagulation of semen: Isolation of •/-glutaminyl-e-lysine dipeptide from clotted secretion protein of guinea pig seminal vesicle, Proc. Natl. Acad. Sci. USA, 69, 2322-2325 (1972). (22) G. E. Siefring, Jr., A. B. Apostol, P. T. Velasco, and L. Lorand, Enzymatic basis for the Ca 2 +- induced cross-linking of membrane proteins in intact human erythrocytes, Biochemistry, 17, 2598- 2604 (1978). (23) L. Lorand, L. K. H. Hsu, G. E. Seifring, Jr., and N. S. Rafferty, Lens transglutaminase and cataract formation, Proc. Natl. Acad. Sci. USA, 78, 1356-1360 (1981). (24) M. M. Buxman, C. J. Lobitz, and K. D. Wuepper, Epidermal transglutaminase, J. Biol. Chem., 255, 1200-1203 (1980). (25) J. E. Folk and J. S. Finlayson, Transglutaminases, Adv. Protein Chem., 31, 1-133 (1977). (26) J. M. Connellay, S. I. Chung, N. K. Whetzel, L. M. Bradley, and J. E. Folk, Structural properties of guinea pig liver transglutaminase, J. Biol. Chem., 246, 1093-1098 (1971). (27) J. E. Folk, J.P. Mullooly, and P. W. Cole, Mechanism of action of guinea pig liver transglutam- inase, J. Biol. Chem., 242, 1838-1844 (1967). (28) M. Gross, N. K. Whetzel, and J. E. Folk, Amine binding sites in acyl intermediates of transglu- taminases, J. Biol. Chem., 252, 3752-3759 (1977). (29) K. Mori, T. Miyamoto, and H. Nakayama (to Kanebo Co., Lt_d_.), Japan Patent Application 1-233519 (1991). (30) M. Satao, Y. Ohtakachi, H. Kamisaka, and M. Suzuki (to Pola Kasei Kogyo Co., Ltd.), Japan Patent Application 1-173275 (1991). (31) T. Miyamoto, (to Kanebo Co., Ltd.), Japan Patent Application 1-25198 (1990). (32) M. Ogawa, N. Ito, and K. Sekiguro (to Ajinomoto Co., Ltd.), Japan Patent Application 2-2771 (1990). (33) V. Iwanij, The use of liver transglutaminase for protein labeling, Eur. J. Blochem., 80, 359-368 (1977). (34) L. Lorand, K. N. Parameswaran, P. Stenberg, Y. S. Tong, P. T. Velasco, N. A. Jonsson, L. Mikiver, and P. Moses, Specificity of guinea pig liver transglutaminase for amine substrates, Bio- chemistry, 18, 1756-1765 (1979). (35) J. Schode and J. E. Folk, Transglutaminase-catalyzed cross-linking through diamines and polyamines, J. Biol. Chem., 253, 4837-4840 (1978). (36) J. E. Folk, M. H. Park, S. I. Chung, J. Schrode, E. P. Lester, and H. L. Cooper, Polyamines as physiological substrates for transglutaminases, J. Biol. Chem., 255, 3695-3700 (1980). (37) H. U. Bergmeyer and H. Beutler, "Ammonia," in Methods of Enzymatic Analysis, Vol. 8, 3rd ed., H. U. Bergmeyer Ed. (VCH, Weinheim 1985), pp. 454-461. (38) L. Lorand, L. K. Campbell-Wilkes, and L. Cooperstein, Anal. Blochem., 50, 623-631 (1972). (39) J. E. Folk and P. W. Cole, Transglutaminase: Mechanistic features of the active site as determined by kinetic and inhibitor studies, Biochim. Biophys. Acta, 122, 244-264 (1966). (40) J. E. Folk and S. I. Chung, Transglutaminases, Methods Enzymol., 113, 358-374 (1985). (41) L. Lorand and S. M. Conrad, Transglutaminases, Mol. Cell. Biochem. 58, 9-35 (1984). (42) P. J. Birckbichler, G. R. Orr, E. Conway, and N. K. Patterson, Transglutaminase activity in normal and transformed cells, Cancer Res., 37, 1340-1344 (1977).
Previous Page Next Page