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Sheila M. Healy

Researcher at University of Arizona

Publications -  9
Citations -  695

Sheila M. Healy is an academic researcher from University of Arizona. The author has contributed to research in topics: Arsenite & Arsenate. The author has an hindex of 7, co-authored 9 publications receiving 680 citations.

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Human monomethylarsonic acid (MMA(V)) reductase is a member of the glutathione-S-transferase superfamily.

TL;DR: It is proposed that MMA(V) reductase and hGSTO 1-1 are identical proteins, which is 100% identical, over 92% of sequence that was analyzed, with the recently discovered human glutathione-S-transferase Omega class hG STO1-1.
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Enzymatic Methylation of Arsenic Compounds: V. Arsenite Methyltransferase Activity in Tissues of Mice

TL;DR: The specific activity of this critical enzyme for arsenite biotransformation was determined by incubating liver, testis, kidney, or lung cytosol of male B6C3F1 mice with sodium arsenite and S-[methyl-3H]adenosyl-L-methionine and measuring the formation of [methyl- 3H]monomethylarsonate.
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Monomethylarsonic acid reductase and monomethylarsonous acid in hamster tissue.

TL;DR: The first-time identification of MMA( III) and DMA(III) in liver after arsenate exposure indicates that the significance of arsenic species in mammalian tissue needs to be re-examined and re-evaluated with respect to their role in the toxicity and carcinogenicity of inorganic arsenic.
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Enzymatic methylation of arsenic compounds: IV. In vitro and in vivo deficiency of the methylation of arsenite and monomethylarsonic acid in the guinea pig.

TL;DR: The guinea pig, like the marmoset and tamarin monkeys and unlike most other animals studied thus far, appears to be deficient as far as the enzyme activities that methylate inorganic arsenite.