90 JOURNAL OF THE SOCIETY OF COSMETIC CHEMISTS e) Increasing the content of solubilizer of solvents decreases the amount of TCC trans- ferred. The effects of refattening agents, i.e., wool wax alcohols on the one hand, and solvent, i.e., dimethylpolyglycolether and solubilizer on the other hand, is certainly the consequence of the increased and decreased chemical potential (or "transfer pressure") of TCC respectively. f) The amounts of TCC transferred (% of the soap used) per second of washing period decrease with the duration of the application period and show a saturation level after about one minute of washing. g) Sniff tests show that soaps containing either 0.26% solubilized TCC or 1.3% pow- dered TCC are equivalent deodorants. REFERENCES (1) German patent DBP 31 37 017 US patent 4 547 307. (2) J. J. Kabara et al., Microdetermination of lipid classes after thin-layer chromatography, Anal. Chem., 48, 814-817 (1976). (3) U. Hoppe, Topologie der Hautoberfliiche, J. Soc. Cosmet. Chem., 30, 213-239 (1979).

j. Soc. Cosmet. Chem., 40, 91-99 (March/April 1989) Electrophoretic analysis of alkylated proteins of human hair from various ethnic groups C. NAPPE and M. KERMICI, L'Oreal, Laboratoires de Recherche Fond•mentale, 1 Avenue Eugene Schueller, 93600 Aulnay sous Bois, France. Received February 1, 1988. Synopsis The general appearance of hair is influenced by many factors, among which the genetic inheritance (ethnic groups) plays a primary role. The structural modification between a blond hair and a curly black hair could be due to either a different genetic protein expression and/or to a different post-translational arrangement during the hair maturation. One approach for addressing such an issue has been to compare the composition of the hair proteins from various human races according to a procedure previously developed by Marshall and Gillespie (1,2). In agreement with the results of these authors, the electrophoresis of Caucasian brown hair shows two groups of proteins: the low-sulfur proteins (LSP), with a MW ranging from 75 Kd to 35 Kd, and the high-sulfur proteins (HSP), with MW ranging from 30 Kd to 14 Kd. The constitutive S-polypeptides of HSP and LSP show the same molecular weights and mobilities for the different samples (European, African, Indian, and Asiatic hairs), but the intensity of HSP was found rather constant, whereas the LSP displayed a very marked difference. The yield in solubilized proteins increases from 0.3% for a Belgian blond hair sample to 19.5% for one sample of French dark brown hair. The darker the hair, the larger the yield in proteins. The variability of intensity of the bands of LSP was found to correlate with the amount of extracted proteins. This study shows that HSP and LSP behave differently with regard to the reducing buffer. These polypep- tides undergo modification after synthesis, and the formation of cross-links in the hair structure might be involved. This study shows that the hair sulfur-containing proteins are identical whatever their racial origin but that the relationship between HSP and LSP varies according to hair color, suggesting different ways of post-translational modification. INTRODUCTION Skin appendages, such as hair, nail, or wool, are composites containing keratin fila- ments embedded in an intracellular matrix (3). Hair proteins can be extracted by re- ducing agents and then derived to more stable derivatives by S-carboxymethylation (SCM). Several approaches to separate SCM proteins have been reported. Using Seph- adex chromatography (4) or analytical electrophoresis (1,5), the alkylated proteins were separated into two major groups: low-sulfur proteins (LSP) and high-sulfur proteins (HSP). From a number of physicochemical studies reviewed by Fraser and Mac Rae (6), it has been concluded that LSP are mostly fibrillar, whereas HSP derive from the hair matrix. Nutritional deficiencies (7), chemical treatments (2), weathering (8), or genetic disorders (9) may induce modification of distribution of SCM proteins which lead to 91