| Literature DB >> 6704178 |
E J Glazenburg, I M Jekel-Halsema, A Baranczyk-Kuzma, K R Krijgsheld, G J Mulder.
Abstract
D-Cysteine, the unphysiological isomer of the sulfur containing amino acid L-cysteine, is not utilized for protein synthesis, glutathione synthesis or taurine production; it was tested as a selective precursor for inorganic sulfate, required for sulfation of xenobiotics. Both cysteine isomers were injected intravenously in the rat, in order to investigate their sulfoxidation to inorganic sulfate. The rates of sulfoxidation were very similar, so that stereospecificity for the amino acid seemed not to play a role. When the rats were fed a low-protein diet (LP-diet; containing only 8% casein as source of amino acids) the serum sulfate concentration decreased to about 20% of control. Under these circumstances the rate of sulfoxidation of both isomers was decreased to the same extent. In order to confirm that both cysteine isomers were equally efficient in providing inorganic sulfate for sulfation of xenobiotics, a constant infusion of harmol (a substrate for sulfation) was given to rats fed the LP-diet. Administration of L- or D-cysteine yielded similar increases in sulfation of harmol under these conditions. These results show that D-cysteine can be used to selectively enhance sulfate availability.Entities:
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Year: 1984 PMID: 6704178 DOI: 10.1016/0006-2952(84)90318-6
Source DB: PubMed Journal: Biochem Pharmacol ISSN: 0006-2952 Impact factor: 5.858