COLLAGEN PEPTIDE SUBSTANTIVITY TO HAIR 43 BO 50 10 V o Vi ,I, ,I, 2.0 o 1.5 • 0.5 • e• ß ß el e ß All ß ß ß ß 60 80 100 120 140 ß 60 B 5O 4O 3O 20 ß •0 %•' ß..• •...• ''- '' '. © A- A-- A-- A-- A-- A --• e A'•A--I'A-•- l e_ e _•_A e_ e.e Ae_ e 60 80 100 120 140 0.6 o 0.4 ,_ •_, 0.2 •øo Fraction No. Figure 2. Elution pattern from Sephadex G-15 of collagen hydrolysate peptides extracted from damaged hair. A) High-temperature or B) High-salt extraction. Monitored fluorescamine (© -- ©) and hydroxypro- line (A -- A) content of protein fractions placed on a G-15 column. Relative fluorescence and hydroxypro- line content in select fractions were monitored as described in Materials and Methods. ture swells the hair structure, allowing exit of adsorbed peptides from the hair shaft, whereas the high salt removes collagen peptides bound via ionic interactions to the hair. ACKNOWLEDGMENTS We acknowledge the work of Dave Simnick in earlier studies related to peptide sub- stantivity to hair. We thank Hank Weightman and Ron Caesar for preliminary amino acid analysis of the peptide fractions. We also thank Barbara Berk for assistance in preparation of this manuscript. REFERENCES (1) E. S. Stern and V. L. Johnsen, Studies on the molecular weight distribution of cosmetic protein hydrolysates, J. Soc. Cosmet. Chem., 28, 447-455 (1977).

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