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Keratins cystine reactivity

Cystine, which contains a disulfide bond, is reported to be the most numerous and reactive amino acid present in hair keratin. Disulfide bonds in cystine are reduced by mercaptans and phosphines, and oxidized by perborates, bromates, and bleach. These reactions result in structural rearrangements within keratin which may affect the physiochemical properties of hair, since disulfide bonds in cystine contribute to the stability of hair. For example, hydrogen peroxide bleaching of hair is an oxidative process which occurs readily in an alkaline medium. This results in the formation of perhydroxy anions which have been proposed to react with cystine to form cysteic acid residues. The process of bleaching results in the loss of approximately 15% of the cystine bonds originally present in keratin and may explain the increased permeability of bleached hair to chemicals. - ... [Pg.79]

IV. Chemical Reactivity of Keratins A. The Reactivity of the Cystine in Keratin... [Pg.247]


See other pages where Keratins cystine reactivity is mentioned: [Pg.120]    [Pg.415]    [Pg.191]    [Pg.337]    [Pg.136]    [Pg.431]    [Pg.433]    [Pg.434]    [Pg.447]    [Pg.454]   
See also in sourсe #XX -- [ Pg.247 , Pg.248 , Pg.249 , Pg.250 , Pg.251 , Pg.252 , Pg.253 , Pg.254 , Pg.255 ]




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