Cystine degradation

Direct measurement of putrefaction is problematic. In laboratory microcosms in which radiolabeled (35S) algae were allowed to settle and decay on top of lake sediments, a net release of less than 5% of the to the water column was observed, and all release occurred within the first 2 weeks (38). However, ongoing microbial uptake of sulfate from the water column may have obscured further release. Maximal potential rates of cystine degradation were estimated by Jones et al. (81) to range from 0.001 to 50 xmol/L per day in Blelham Tarn sediments and by Dunnette (82) to range from 28 to 47 xmol/L per day in sediments from two lakes. Similar measurements of potential rates of hydrolysis of sulfate esters (83) tremendously overestimated the rates calculated by mass balance to occur in sediments of Wintergreen Lake (73). A better understanding of putrefaction is needed to predict retention and concentrations of S in sediments. 

Autosomal recessive cystinosis is caused by an enzyme-induced blockage of cystine degradation, particularly in the RES lysosomes of the bone marrow, liver, spleen and kidneys. Especially in the stellate cells of the spleen and to a lesser extent of the hepatic lobule centres, hexagonal and rectangular cystine crystals are found, pointing at an early stage to cystinosis. There is evidence of hepatosplenomegaly and microvesicular steatosis. The clinical picture of the infantile type presents as a Fan-coni syndrome, (s. pp 593, 597) The children affected die in the first five years of life. 

Cysteine [52-90 ] is a thiol-bearing amino acid which is readily isolated from the hydrolysis of protein. There ate only small amounts of cysteine and its disulfide, cystine, in living tissue (7). Glutathione [70-18-8] contains a mercaptomethyl group, HSCH2, and is a commonly found tripeptide in plants and animals. Coenzyme A [85-61-0] is another naturally occurring thiol that plays a central role in the synthesis and degradation of fatty acids. 

In the case of the thiopurines the electrochemical processes do not appear to agree at all with the known biological oxidations. However, again in the case of 6-thiopurine not even a complete picture of the metabolites is available. The electrochemical data indicates that thiopurines are very readily oxidized to disulfides and hence to sulfinic or sulfonic acids. In view of well-known sulfide-disulfide transformations in biological situations (e.g., L-cy-steine to L-cystine), it is not unlikely that part of the metabolic degradation pathway for thiopurines might proceed via reactions of the sulfide moiety. 

Permonosulphuric acid treatment confers only a modest shrink-resist effect which usually needs to be improved by a subsequent additive treatment. It has been suggested [300] that the most likely mechanism for inhibiting felting by permonosulphuric acid treatment is the removal of degraded protein from below the exocuticle, producing a modified surface with a reduced differential friction. The direct formation from cystine residues of low concentrations of Bunte salts has been confirmed, as indicated in Scheme 10.42. 

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]. 

Standard hydrolysis is performed with 6M HC1 at 110°C for 24 hJ2 But the method can be varied in terms of acids used, temperature, and time, as well as in the mode of gas- or liquid-phase hydrolysis (Table 1). Time-dependent hydrolysis is required to determine the exact stoichiometry for unstable amino acids as well as for particular sequences difficult to hydrolyze. Tryptophan, methionine, cystine, tyrosine, serine, and threonine are known to be degraded at an extent of >50, >50, >30, >20, >10, and >5%, respectively.141 Therefore, performing standard hydrolysis for 24, 48, and 72 h, and extrapolation to zero time of hydrolysis allows for better quantitation of these unstable amino acids, whereas extrapolation... 

The problems encountered are numerous. Tryptophan is highly prone to degradation in acid digestions. This is especially the case in food analysis, where samples often contain significant quantities of carbohydrates that greatly exacerbate tryptophan s degradative tendencies. Cyst(e)ine is partially oxidized during acid hydrolysis and will likely be found in several forms cystine, cysteine, cysteine sulfinic acid, and cysteic acid. Methionine can be partially lost in simi-... 

A maltol-ammonia browning reaction produced thirteen pyrazines, two pyrroles, two oxazoles, and one pyridine (12). The major products of this system were 2-ethyl-3-hydroxy-6-methylpyridine and 2-ethyl-3,6-dimethylpyrazine. It is difficult to construct possible formation mechanisms for these compounds from maltol and ammonia. All the carbon atoms must come from maltol. It is possible, then, that maltol degrades into smaller carbon units and that these fragments recombine to form larger carbon units, producing these compounds. Recently, the formation of thiophenones and thiophenes from the reaction of 2,5-dimethyl-4-hydroxy-3(2H)-furanone and cysteine or cystine was reported (13. 14). All these reaction mixtures were reported to possess a cooked meat-like flavor. 

Recently, we reported on the thermal degradation of cystine (21) and also the thermal degradation of DMHF (22) as background for the title reaction. 

The volatile components identified from the reaction of cystine and DMHF in aqueous medium are shown in Table I. 2,4-Hexanedione, 3,5-dimethyl-l,2,4-trithiolanes and thiophenes are the major compounds. The mechanistic relationship of the three thiophenones produced has been postulated (23). The major groups of volatile components identified from the reaction in the glycerol medium are 1,3-dioxolanes and thiazoles (Table II). 1,3-Dioxolanes are formed by the reaction of glycerol and the degraded carbonyls by ketal or acetal formations. Comparison of the reaction of cystine and DMHF in water and in glycerol is outlined in Table III. 

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