| ID | 32415 |
| JaLCDOI | |
| FullText URL | |
| Author |
Kiguchi, Shozo
|
| Abstract | Metabolism of 3-mercaptopyruvate was investigated using homogenates of rat heart, liver and kidney. When 3-mercaptopyruvate was incubated with heart homogenate, L-cysteine, L-alanine, S-(2-hydroxy-2-carboxyethylthio)-L-cysteine and 3-mercaptolactate were produced. At the same time, a decrease in the amounts of L-glutamate and L-aspartate was demonstrated. These results indicate that 3-mercaptopyruvate was converted to L-cysteine by cysteine aminotransferase (EC 2.6.1.3), to 3-mercaptolactate by lactate dehydrogenase (EC 1.1.1.27), and to pyruvate by 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2), and that HCETC and L-alanine were formed from these products. In the presence of liver homogenate, 3-mercaptopyruvate was mainly metabolized by 3-mercaptopyruvate sulfurtransferase; production of L-cysteine was small and HCETC was not formed. The metabolism of 3-mercaptopyruvate in the presence of kidney homogenate was intermediate between heart and liver: a fair amount of L-cysteine was formed, but HCETC was not produced. A peak which corresponds to L-cysteine-glutathione disulfide on the chromatogram of amino acid analysis was present when 3-mercaptopyruvate was incubated with heart or liver homogenate, but not with kidney homogenate. |
| Keywords | 3-mercaptopyruvate
L-cysteine
3-mercaptolactate
S-(2-hydroxy-2-carboxyethylthio)-L-cysteine
L-cysteine-glutathione disulfide
|
| Amo Type | Article
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| Publication Title |
Acta Medica Okayama
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| Published Date | 1983-04
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| Volume | volume37
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| Issue | issue2
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| Publisher | Okayama University Medical School
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| Start Page | 85
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| End Page | 91
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| ISSN | 0386-300X
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| NCID | AA00508441
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| Content Type |
Journal Article
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| language |
English
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| File Version | publisher
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| Refereed |
True
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| PubMed ID | |
| Web of Science KeyUT |