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zeige Details Trelstad, Robert L., Lawley, Karen R., ... Nonenzymatic hydroxylations of proline and lysine by reduced oxygen derivatives
in: Nature . - London [u.a.] : Nature Publising Group, ISSN 1476-4687, Vol. 289, No. 5795 (1981), p. 310-312
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1981
The biosynthesis of trans-3- and trans-4-hydroxyprolines and 5-hydroxylysine in animal cells requires polypeptide proline or lysine, enzymes and cofactors including iron, and possibly involves peroxidatic intermediates1. Several laboratories have reported the presence of low-molecular-weight hydroxyproline and hydroxylysine peptides in cell and organ cultures2–5. We found that these small peptides contained the trans-3 and cis-4 isomers of hydroxyproline as well as trans-4 ones and that their production was not completely inhibited by α, α-dipyridyl, an iron chelator and effective inhibitor of enzyme-mediated hydroxylations5. It is known that oxygen or hydrogen peroxide in the presence of metal can hydroxylate proline and other aromatic compounds6–11. We show here that reduced oxygen derivatives can hydroxylate both free and poly peptide-bound proline and lysine, and that scavengers of hydroxyl radicals suppress, but do not completely inhibit, this reaction. Reduced oxygen derivatives can be generated in normal and pathological circumstances12, and some of the low-molecular-weight hydroxyproline and hydroxylysine peptides found in cell and organ cultures might be derived from these derivatives and therefore do not reflect collagen turnover, but rather some other cellular activity.
beteiligte Personen: Trelstad, Robert L. , Lawley, Karen R. , Holmes, Lewis B.
Format: Elektronisch
Erschienen: 1981.
Serie: Nature Archives 1869 - 2007 [Dig. Serial]
Schlagwörter:
URL: http://dx.doi.org/10.1038/289310a0

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