
doi: 10.1007/bf02783907
pmid: 10328340
Biotransformation of inorganic arsenic in mammals is catalyzed by three serial enzyme activities: arsenate reductase, arsenite methyltransferase, and monomethylarsonate methyltransferase. Our laboratory has purified and characterized these enzymes in order to understand the mechanisms and elucidate the variations of the responses to arsenate/arsenite challenge. Our results indicate a marked deficiency and diversity of these enzyme activities in various animal species.
Adenosine Triphosphatases, Mammals, Arsenites, Arsenite Transporting ATPases, Ion Pumps, Methyltransferases, Methylation, Catalysis, Species Specificity, Multienzyme Complexes, Enzyme Induction, Animals, Biotransformation
Adenosine Triphosphatases, Mammals, Arsenites, Arsenite Transporting ATPases, Ion Pumps, Methyltransferases, Methylation, Catalysis, Species Specificity, Multienzyme Complexes, Enzyme Induction, Animals, Biotransformation
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 38 | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Top 10% | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |
