Keratins oxidation

Keratin hydrolysates, reaction prods, with cocoacyl chloride. See Cocoyl hydrolyzed keratin Keratin, hydrolyzed. See Hydrolyzed keratin Keratin, oxidized. See Oxidized keratin Keratins, hydrolysates. See Hydrolyzed keratin Keratins, hydrolysates, reaction prods, with capryloyl chloride. See Capryloyl hydrolyzed keratin... 

Oxidized L-cysteine. See L-Cystine Oxidized keratin Synonyms Keratin, oxidized Definition Material derived chemically from keratin by oxidation with hydrogen peroxide Uses Hair conditioner, skin conditioner in cosmetics... 

Two major types of muscle fibers are found in humans white (anaerobic) and red (aerobic). The former are particularly used in sprints and the latter in prolonged aerobic exercise. During a sprint, muscle uses creatine phosphate and glycolysis as energy sources in the marathon, oxidation of fatty acids is of major importance during the later phases. Nonmuscle cells perform various types of mechanical work carried out by the structures constituting the cytoskeleton. These strucmres include actin filaments (microfilaments), micrombules (composed primarily of a- mbulin and p-mbulin), and intermediate filaments. The latter include keratins, vimentin-like proteins, neurofilaments, and lamins. 

Dichromate anions are readily absorbed under acidic conditions by wool that has been dyed with chrome dyes. The chromium(VI) on the fibre is then gradually reduced by the cystine residues in wool keratin to chromium(III) cations, which react with the dye ligands to form a stable complex. In this way the cystine disulphide bonds are destroyed, resulting in oxidative degradation of the wool fibres [71]. 

Cysteine disulfide formation is one of the most important posttranslational modifications involved in protein structure. Disulfides play a crucial role in maintaining the structure of many proteins including insulin, keratin, and many other structurally important proteins. While the cytoplasm and nucleus are reducing microenvironments, the Golgi and other organelles can have oxidizing environments and process proteins to contain disulfide bonds (Scheme 5). 

The surface of a wool hair is covered by keratin sheds, which cause a distinct tendency to shrinkage and formation of felts. This behavior is usually undesirable and thus an antifelt finishing is the most important treatment during the processing of woolen textiles. One of the most important standard procedures, the Hercosett finish, is based on the oxidative treatment of wool by application of compounds that release chlorine. Examples for applied chemicals are NaOCl, CI2 gas, and dichloroisocyanuric acid (DCCA) [14]. 

Similar keratin filaments are found in hair. In a single wool fiber with a diameter of about 20 pm, millions of filaments are bundled together within dead cells. The individual keratin helices are cross-linked and stabilized by numerous disulfide bonds (see p. 72). This fact is exploited in the perming of hair. Initially, the disulfide bonds of hair keratin are disrupted by reduction with thiol compounds (see p. 8). The hair is then styled in the desired shape and heat-dried. In the process, new disulfide bonds are formed by oxidation, which maintain the hairstyle for some time. 

Limited experience with humans has shown that exposure to even small amounts of the higher chlorinated derivatives, particularly hexachlorodiphenyl oxide, may result in appreciable acneform dermatitis. Chloracne is usually persistent and affects the face, ears, neck, shoulders, arms, chest, and abdomen (especially around the umbilicus and on the scrotum). The most sensitive areas are below and to the outer side of the eye (malar crescent) and behind the ear. The skin is frequently dry with noninflammatory comedones and pale yellow cysts containing sebaceous matter and keratin. 

It is evident that specific residue-related features observed in the rod domain of one particular IF chain type are frequently not observed in the same place (if at all) in the other chain types and, of course, the large differences in head and tail structure and sequence between chain types preclude identical roles from occurring there as well. The highly specialized sequence characteristics thus define unique structural assemblies and functions, while still maintaining a high degree of structural uniformity, particularly in the manner of rod domain assembly. Even in this case, small but important differences in the An, A22, and A12 modes occur. Distinct IF structures have been identified for (1) unoxidized trichocyte keratin and epidermal keratin (2) oxidized trichocyte keratin (3) Type III and IV IF proteins and (4) the nuclear lam ins. 

In the second method, a metal salt solution (silver, lead, or bismuth less often nickel, cobalt, or manganese) is applied colloidal sulfur may also be added. Dyeing is based on (1) The reaction of the metal salts with the added sulfur and the sulfur in the hair keratin, which yields metal sulfides, and (2) The deposition of finely divided metals or metal oxides. With these products progressive coloration also is obtained. 

Permanent hair colors can be achieved with tint shampoos. The shampoo base is adjusted to an alkaline pH and contains oxidation dye intermediates. Before application, it is mixed with hydrogen peroxide or a hydrogen peroxide addition compound. In comparison with oxidation hair dyes, tint shampoos employ lower concentrations of base and oxidant. This suppresses the simultaneous bleaching process that occurs during dyeing (see Section 5.4.2). As a result, damage to the keratin in hair is diminished, but the uniform coloring action is lost. 

Melanin granules are secreted by melanocytes in the hair papilla and distributed to keratin in the hair cortex and inner layers of the hair sheath during normal development. Melanogenesis is subject to hormonal control and has been the focus of intensive genetic studies. Two main forms of melanin exist in human skin—eumelanin and phaeomelanin, both of which are derived from tyrosine through the action of tyrosinase (a cupro-enzyme) and possibly other key enzymes (with nickel, chromium, iron, and manganese as cofactors). Tyrosine is converted to dihydroxyphenylalanine and, via a series of intermediate steps, to indole-5,6-quinone, which polymerizes to eumelanin. Phaeomelanins are produced by a similar mechanism but with the incorporation of sulfur (as cysteine) by a nonenzymatic step in the oxidation process. 

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. - ... 

A furylmethyl group has been incorporated into a dye developer-coupler combination which has been shown to be useful for the oxidative dyeing of keratin fibers, especially human hair <2002W02072568>. The regioisomeric furans 29 and 30 belong to this class of compounds and are easily synthesized from the corresponding aldehydes and a previously generated aminophenyl carbamate. 

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