18 JOURNAL OF COSMETIC SCIENCE Table I Amino Acid Compositions of Extracted Fractions From the Root End a Determined in this study Literature 2 M extract 0.4 M extract HMW b Residue Matrix • MicrofibriF Cuticle d Lysine 0.6 3.5 2.0 3.1 0.6 3.5 3.4 Histidine 1.0 0.7 0.5 1.2 0.9 0.7 0.5 Arginine 6.6 5.4 7.0 4.6 5.4 7.1 2.6 Half-cystine e 23.5 9.0 10.1 19.1 27.2 7.6 18.1 Aspartic acid 2.9 8.3 5.9 3.1 2.5 9.3 3.2 Threonine 10.7 6.9 7.9 6.2 10.3 5.4 4.6 Serine 12.0 8.0 11.8 12.6 11.9 8.9 16.1 Glutamic acid 8.4 17.2 12.4 6.4 8.4 16.5 8.9 Proline 12.3 5.1 9.1 7.5 12.7 3.8 10.5 Glycine 6.2 5.2 6.3 11.4 6.1 5.1 8.8 Alanine 2.0 6.3 5.3 4.6 2.3 6.9 5.4 Valine 5.5 6.0 7.0 6.7 5.2 6.1 7.3 Methionine 0.0 1.1 0.2 0.9 0.0 0.4 0.5 Isoleucine 2.0 3.6 3.4 3.0 1.8 3.6 2.2 Leucine 3.3 9.2 7.1 5.5 2.2 10.2 4.5 Tyrosine 1.6 2.5 2.7 2.4 1.5 2.5 2.1 Phenylalanine 1.4 2.0 1.8 1.9 1.1 1.9 1.2 All values are the mean of three experiments. Refer to Figure 1 for experimental conditions. Expressed as residues per 100 residues. High-molecular-weight protein from the tip end of perreed hair. Reduction following alkylation and isoelectrical precipitation method (9). d Physical isolation method (15). Estimated as cysteic acid converted by performic acid. study, we applied this method to the analysis of hair components, but it could also be applied to the reconstitution of the intermediate filament because the disulfide bond easily reforms using only dialysis. ANALYSIS OF THE DAMAGED COMPONENTS OF PERMED HAIR The cortical proteins. We applied the developed method to the analysis of hairs from individual persons. The hair from three women, labeled "no treatment," was the hair that had not been exposed to any cosmetic treatment, and Type I and Type II were the hairs that had been permed every two or three months. More than 80% of the Type I hair had split ends, while the Type II hair scarcely had any split ends but contained broken hairs. The SEM micrographs of the tip ends of these hairs are shown in Figure 5. Table II shows the contents of each fraction, from the root end to the tip end. The data are the mean of three examinations. On the root end, the compositions of three hairs were very similar. The "no treatment" hair showed almost the same composition toward the tip end, but the perreed hairs apparently changed. The microfibril protein signifi- cantly decreased, while the high-molecular-weight protein and the residue increased. On the other hand, the matrix protein slowly decreased whether or not the hair had been permed. As shown later, the cuticle layers actually decreased, and the increase in residue means an increase in the insoluble proteins (9). It is reported that alkaline pH will form irregular cross-linking such as lanthionine (17). We considered that the "intact" mi- crofibril protein had partially turned into the insoluble protein and decreased.

DAMAGED COMPONENTS OF PERMED HAIR 19 .,. Figure 4. Scanning electron micrographs of the hairs after extraction: (a) 2 M 2-ME extraction and (b) successive extraction by 0.4 M 2-ME following (a). Refer to Figure 1 for detail. O rb c 11•711 14KV X700 49um 11•708 14K¾ X50e 6eum Figure 5. Scanning electron micrographs of the tip end of individual hairs: (a) "No treatment," (b) Type I, and (c) Type II. "No treatment" means the hair has not been exposed to any chemical treatment. "Type I" and "Type II" mean the hair has been permed every two or three months. The cuticle. The abrasion of the cuticle layers by brushing, combing, etc., has been reported in the literature. We developed a quantitative analysis method using the determination of the IP, which exists only in the exo- and endo-cuticles (18), and the MEA, which exists only in the cell membrane complex (CMC) of the cuticle (19), as indicators. A summary of the results is given in Table III. The IP amount decreased toward the tip end similarly in all three hair types, while perming slightly accelerated the damage of the cuticular proteins. On the other hand, the amount of MEA decreased faster in Type II hair than in other hair types. When viewed using the SEM, the cuticle