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Cystine reduction

Microemulsions have also been investigated for the use in chemical hair treatment [14]. Permanent wave products are based on the reduction of hair keratine cystine, which weakens the protein structure and allows a manipulation of the hair shape. Savelli et al. compared the cystine reduction obtained by thioglycolic acid in water with that obtained by a microemulsion. The microemulsion is based on the anionic surfactant sodium dode-cylsulphate, the co-surfactant pentanol and dodecane as the unpolar oil component. The cysteine formation is evaluated over a time period of 5 min. The experimental data are... [Pg.234]

This latter system appears to be the one dominant in cystine reduction by mammalian cells. [Pg.313]

Two human genetic diseases are known which involve this disulphide amino acid. In one, cystinuria , there is a transport defect in the intestine and kidney. This results in abnormally high levels of cystine in the urine and can result in the precipitation of cystine crystals and kidney stone formation. In cystinosis, cystine crystals form within cells and eventually cause severe kidney damage. The nature of the primary biochemical lesion is unknown all known cystine reduction systems of the cell appear to be normal. [Pg.313]

Cystine reduction by sulfitolysis is generally preferred for processing and derivatiza-tion of cosmetic proteins, because it takes places at slightly acidic pH and room temperature, with no degradation of other amino acids. [Pg.434]

The reagent most frequently used for the reduction of hair is thioglycolic acid [68-11-1]. Although a variety of other mercaptans have been screened (51), none has been able to match the unique combination of efficacy, safety, and low cost that is a hallmark of thioglycolic acid. The use of microemulsions and their effectiveness on cystine reduction obtained by thioglycolic acid as compared to water has been investigated. An anionic surfactant, sodium dodecylsulfate, has shown to be less effective than that of water for permanent wave formulations. However, surfactants based on nonionic surfactants are less irritating (52). [Pg.115]

HSCH -CHNHj-COjH. Cysteine is a reduction product of cystine. It is the first step in the breakdown of cystine in the body, one molecule of cystine splitting to give two molecules of cysteine. Cysteine is soluble in water but the solution is unstable, and is reoxidized to cystine. [Pg.124]

The differences in the amino acid chemistry of the hide coUagen and the hair keratin are the basis of the lime-sulfide unhairing system. Hair contains the amino acid cystine. This sulfur-containing amino acid cross-links the polypeptide chains of mature hair proteins. In modem production of bovine leathers the quantity of sulfide, as Na2S or NaSH, is normally 2—4% based on the weight of the hides. The lime is essentially an unhmited supply of alkah buffered to pH 12—12.5. The sulfide breaks the polypeptide S—S cross-links by reduction. Unhairing without sulfide may take several days or weeks. The keratin can be easily hydrolyzed once there is a breakdown in the hair fiber stmcture and the hair can be removed mechanically. The coUagen hydrolysis is not affected by the presence of the sulfides (1—4,7). [Pg.83]

Disulfides. As shown in Figure 4, the and h-chains of insulin are connected by two disulfide bridges and there is an intrachain cycHc disulfide link on the -chain (see Insulin and other antidiabetic drugs). Vasopressin [9034-50-8] and oxytocin [50-56-6] also contain disulfide links (48). Oxidation of thiols to disulfides and reduction of the latter back to thiols are quite common and important in biological systems, eg, cysteine to cystine or reduced Hpoic acid to oxidized Hpoic acid. Many enzymes depend on free SH groups for activation—deactivation reactions. The oxidation—reduction of glutathione (Glu-Cys-Gly) depends on the sulfhydryl group from cysteine. [Pg.379]

U. T. Ruf gg u. J. Rudinger, Reductive Cleavage of cystine disulfides with tributylphosphins, Methods Enzymol. 47, 111 (1977). [Pg.784]

The first reductive kinetic resolution of racemic sulphoxides was reported by Balenovic and Bregant. They found that L-cysteine reacted with racemic sulphoxides to produce a mixture of L-cystine, sulphide and non-reduced optically active starting sulphoxide (equation 147). Mikojajczyk and Para reported that the reaction of optically active phosphonothioic acid 268 with racemic sulphoxides used in a 1 2 ratio gave the non-reduced optically active sulphoxides, however, with a low optical purity (equation 148). It is interesting to note that a clear relationship was found between the chirality of the reducing P-thioacid 268 and the recovered sulphoxide. Partial asymmetric reduction of racemic sulphoxides also occurs when a complex of LiAlH with chiral alcohols , as well as a mixture of formamidine sulphinic acid with chiral amines, are used as chiral reducing systems. ... [Pg.296]

Walsh et al. (2000) have reported the reduction of L-cystine hydrochloride to L-cysteine hydrochloride and have covered laboratory kinetics to process modelling for several m cells. [Pg.168]

The first step in this reaction is connected with breaking of the O—O bond, with a markedly unsymmetrical energy profile (a 0.2). Other reactions connected with a similar bond breakage have an analogous course, e.g. the reduction of cystine at a mercury electrode. [Pg.371]

A development reported recently [519] involves reduction of the cystine disulphide bonds in wool with either thioglycolic acid or tetrakis(hydroxymethyl)phosphonium chloride to form thiol groups, followed by crosslinking with bifunctional reactive dyes. This gave improved insect resistance but had adverse effects on physical properties such as strength, shrinkage and stiffness, thus limiting the potential of the process for commercial use. [Pg.276]

Cysteine sulfhydryls and cystine disulfides may undergo a variety of reactions, including alkylation to form stable thioether derivatives, acylation to form relatively unstable thioesters, and a number of oxidation and reduction processes (Figure 1.10). Derivatization of the side chain sulfhydryl of cysteine is one of the most important reactions of modification and conjugation techniques for proteins. [Pg.10]

One of the most convenient ways of generating sulfhydryl groups is by reduction of indigenous disulfides. Many proteins contain cystine disulfides that are not critical to structure or activity. [Pg.87]

Dithiothreitol (DTT) and dithioerythritol (DTE) are the trans and cis isomers of the compound 2,3-dihydroxy-1,4-dithiolbutane. The reducing potential of these versatile reagents was first described by Cleland in 1964. Due to their low redox potential (—0.33 V) they are able to reduce virtually all accessible biological disulfides and maintain free thiols in solution despite the presence of oxygen. The compounds are fully water-soluble with very little of the offensive odor of the 2-mercaptoethanol they were meant to replace. Since Cleland s original report, literally thousands of references have cited the use of mainly DTT for the reduction of cystine and other forms of disulfides. [Pg.88]

Small molecules containing disulfide bonds (such as cystine-containing peptides) may be reduced and isolated simply by removing the immobilized reductant. Separation of reduced molecules from reductant is much more difficult if a soluble reducing agent is used with low-molecular-weight disulfides. [Pg.97]

Harry B. Gray and Walther Ellis,13 writing in Chapter 6 of reference 13, describe three types of oxidation-reduction centers found in biological systems. The first of these, protein side chains, may undergo oxidation-reduction reactions such as the transformation of two cysteine residues to form the cystine dimer as shown in equation 1.28 ... [Pg.20]

L-Cysteine is a high value a-amino acid used world-wide in a scale of 1200-15001 year-1 as additive in foodstuffs, cosmetics or as intermediate or active agent (as antidote to several snake venoms) in the pharmaceutical industry. Chemical routes generally lack the efficiency of electrochemical techniques, or they produce mixtures of l- and d- forms rather than the L-isomer. The most common electrochemical route is the cathodic reduction of L-Cystine in acid (usually HC1) solution to produce the stable hydrochloride. In Table 10, the charateristic data for a laboratory bench, laboratory pilot and a product pilot reaction using a DEM filter press are compared [13]. A production scale study was carried out in a filterpress reactor divided by a cation exchange membrane with a total area of 10.5 m2. The typical product inventory was 450 kg/24-hour batch time. For more details see Ref. [13]. [Pg.153]

Hitchman ML, Millington JP, Ralph TR, Walsh FC (1989) The electrochemical reduction of cystine to L-cysteine, I Chem E Symp Ser 112 222... [Pg.229]

The A and B peptide chains in insulin are linked through disulfide bridges. Their presence was suspected from the change in molecular weight which followed the reduction of insulin. For quantitative analyses the S-S bridges had to be broken. Sanger, following the approach used by Toennies and Homiller (1942), oxidized the protein with performic acid, so that the half-cystines were converted to cysteic acid. After oxidation, insulin could be separated into its A and B chains, the A peptide with 20 amino acid residues and the B with 30. [Pg.178]


See other pages where Cystine reduction is mentioned: [Pg.973]    [Pg.973]    [Pg.254]    [Pg.145]    [Pg.313]    [Pg.4593]    [Pg.354]    [Pg.973]    [Pg.973]    [Pg.254]    [Pg.145]    [Pg.313]    [Pg.4593]    [Pg.354]    [Pg.459]    [Pg.459]    [Pg.459]    [Pg.459]    [Pg.296]    [Pg.191]    [Pg.339]    [Pg.87]    [Pg.148]    [Pg.358]    [Pg.80]    [Pg.84]    [Pg.88]    [Pg.436]    [Pg.828]    [Pg.1109]    [Pg.937]    [Pg.100]    [Pg.17]    [Pg.125]    [Pg.506]   
See also in sourсe #XX -- [ Pg.106 ]

See also in sourсe #XX -- [ Pg.374 ]

See also in sourсe #XX -- [ Pg.239 ]




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