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Cystine



  

Cystine

Systematic (IUPAC) name
Cystine
Identifiers
PubChem          ?
Chemical data
Formula C6H12N2O4S2 
Molar mass 238.32
Complete data

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.[1] 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.[2]

Additional recommended knowledge

Contents

Properties

The disulfide link is readily reduced to give the corresponding thiol, cysteine. This reaction is typically effected with thiols such as mercaptoethanol or dithiothreitol.

(SCH2CH(NH2)CO2H)2 + 2 RSH → 2 HSCH2CH(NH2)CO2H + RSSR

Nutritional sources

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

Disulfide bonds can be broken at temperatures above about 150 °C, especially at low moisture levels (below about 20%)[3].

Side effects

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.[citation needed]

See also

References

  1. ^ "cystine." Encyclopædia Britannica. 2007. Encyclopædia Britannica Online. 27 July 2007 www.britannica.com/eb/article-9028437/cystine
  2. ^ Gortner, R. A.; W. F. Hoffman, W. F. (1941). "l-Cystine". Org. Synth.; Coll. Vol. 1: 194. 
  3. ^ M.A. Aslaksena, O.H. Romarheima, T. Storebakkena and A. Skrede (28 June 2006). "Evaluation of content and digestibility of disulfide bonds and free thiols in unextruded and extruded diets containing fish meal and soybean protein sources". Animal Feed Science and Technology 128 (3-4): 320-330.
 
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.
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