| Autor: |
Shoeman DW; Medical Research Laboratories, VA Medical Center, Minneapolis, MN 55417 USA., Shirota FN, DeMaster EG, Nagasawa HT |
| Jazyk: |
angličtina |
| Zdroj: |
Alcohol (Fayetteville, N.Y.) [Alcohol] 2000 Jan; Vol. 20 (1), pp. 55-9. |
| DOI: |
10.1016/s0741-8329(99)00056-7 |
| Abstrakt: |
Nitroxyl (HNO) is the aldehyde dehydrogenase (AIDH) inhibitor produced by catalase action on cyanamide. Incubation of N-acetyl-L-cysteine (NAC), a reagent with a free sulfhydryl group, with Piloty's acid (a nitroxyl generator) suggested that NAC was acting as a competitive "trap" for nitroxyl. Elucidation of the structure of this reaction product should give an insight as to how nitroxyl interacts with AIDH, a sulfhydryl enzyme. We now present evidence that the product formed is N-acetyl-L-cysteinesulfinamide (NACS). We have synthesized NACS and showed that this synthetic product was identical to the product formed in the trapping experiment. Both had identical RT values by reverse phase HPLC and identical RF values by TLC using three different solvent systems. The structural identification of this nitroxyl trapped product as a sulfinamide now allows the chemical confirmation of the active-site cysteine residue of AIDH as Cys-302. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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