JOURNAL OF COSMETIC SCIENCE 462 which relates to the amount of cuticle-to-cuticle overlap and to the relative amounts of cuticle–cuticle CMC versus cuticle–cortex CMC versus cortex–cortex CMC. The Allworden reaction can be produced on both wool fi ber and human hair (29). Although the reaction appears different on human hair than wool fi ber, Bradbury and Leeder (15) have shown that this is because of much greater scale overlap on human hair, where only about 1/5th to 1/6th of each cuticle cell shows on the surface of hair fi bers, and they explain that Merino wool contains only a single layer of cuticle scales, with approximately 5/6th of each scale in the surface and only about 1/6th scale overlap (29) on the surface. Individual cuticle cells have also been isolated from wool, human hair, and several other keratin fi bers, and have been shown to behave similarly to chlorine water (29). 18-MEA accounts for 40–50% of the covalently bound fatty acids in human hair and wool fi ber (35) and it is at- tached to the top surface of cuticle cells in both fi bers (11). Table I shows that the covalently bound fatty acids are similar in both human hair and wool fi ber and that covalently bound fatty acids are in the cuticle–cuticle CMC but not in the cortex in both of these fi bers. The compositions of the solvent-extractable lipids of both fi bers are similar, consisting primarily of fatty acids, cholesterol, cholesterol sulfate, and ceramides (34,35). Further- more, these lipids are extractable from both human hair and wool fi ber with chloroform/ methanol/aqueous potassium chloride, and liposomes can be generated from these ex- tracts (48). Furthermore, these extracted lipids represent the main ingredients in the cortex–cortex CMC, and they are very similar in both fi bers. And last, but not least, the effects of chemical and photochemical reactions and physical stresses are similar for the CMCs of both of these fi bers, as shown in “Chemical and Physical Actions on the CMC of Hair,” in this review. Perhaps, with additional research, signifi cant structural and/or re- activity differences between the CMCs of human hair and wool fi ber will become more apparent, but they are not apparent today. REFERENCES (1) G. E. Rogers, Electron microscope studies of hair and wool, Ann. N.Y. Acad. Sci., 83, 378–399 (1959). (2) G. E. Rogers, Electron microscopy of wool, J. Ultrastruct. Res., 2, 309–330 (1959). (3) R. D. B. Fraser, T. P. MacRae, G. Rogers, et al., in Keratins: Their Composition, Structure and Biosynthesis, I. N. Kugdmass, Ed. (C. C. Thomas, Springfi eld, Ill., 1972), Ch. 4. (4) C. Robbins et al., Failure of intercellular adhesion in hair fi bers with regard to hair condition and strain conditions, J. Cosmet. Sci. 55, 351–371 (2004). (5) W. G. Bryson, B. R. Herbert, D. A. Rankin, and G. L. Krsinic, Characterization of proteins obtained from papain/dithiothreitol digestion of Merino and Romney wools, Proc. 9th IWTRC, Biella, Italy, 1995, pp. 463–473. (6) A. J. Swift and J. Holmes, Degradation of human hair by papain. III. Some electron microscope ob- servations, Textile Res. J., 35, 1014–1019 (1965). (7) A. J. Swift, Human hair cuticle: Biologically conspired to the owner’s advantage, J. Cosmet. Sci. 50, 23–47 (1999). (8) Y. Nakamura et al., Electrokinetic studies on the surface structure of wool fi bres, Proc. 5th, IWTRC, Aachen, 5, 34–43 (1975). (9) R. D. B. Fraser, T. P. MacRae, and G. E. Rogers, in Keratins: Their Composition, Structure and Biosynthesis, I. N. Kugdmass, Ed. (C. C. Thomas, Springfi eld, Ill., 1972), pp. 70–75. (10) L. N. Jones and D. E. Rivett, Effects of branched chain 3-oxo acid dehydrogenase defi ciency on hair in maple syrup urine disease, J. Invest. Dermatol., 104, 688 (1995). (11) L. N. Jones and D. E. Rivett, The role of 18-methyleicosanoic acid in the structure and formation of mammalian hair fi bers, Micron, 28, 469–485 (1997).

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