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Cystine is the amino acid formed when of a pair of cysteine molecules are joined by a disulfide bond. It is described by the formula (SCH2CH(NH2)CO2H)2. It is a colorless solid, and melts at 247-249 °C. It was discovered in 1810 by William Hyde Wollaston but was not recognized as a component of proteins until it was isolated from the horn of a cow in 1899. Through formation of disulfide bonds within and between protein molecules, cystine is a significant determinant of the tertiary structure of most proteins. Disulfide bonding, along with hydrogen bonding and hydrophobic interactions is partially responsible for the formation of the gluten matrix in bread. Human hair contains approximately 5% cystine by mass.
Supplemental N-acetyl cysteine is claimed to be a source of cystine, but the dose of this supplement is limited by side effects. One of the richest nutritional sources of cystine in the diet is undenatured whey proteins from milk. The disulfide-bonded cystine is not digested or significantly hydrolized by the stomach, but is transported by the blood stream to the tissues of the body. Here, within the cells of the body, the weak disulfide bond is cleaved to give cysteine, from which glutathione can be synthesized.
In animal feed
Nutritional sources of cystine are virtually free of the toxic side effects associated with the single molecule of cysteine, N-acetyl cysteine. The greatest dietary source of cystine is bio-active, unpasteurized or low-heat pasteurized undenatured whey proteins.
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Cystine". A list of authors is available in Wikipedia.|