Linked Life Data

10604879

Source:http://linkedlifedata.com/resource/pubmed/id/10604879

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2000-2-17
pubmed:abstractText
A unique enzyme, MMA(V) reductase, has been partially purified from rabbit liver by using DEAE-cellulose, carboxymethylcellulose, and red dye ligand chromatography. The enzyme is unique since it is the rate-limiting enzyme in the biotransformation of inorganic arsenite in rabbit liver. The K(m) and V(max) values were 2.16 x 10(-)(3) M and 10.3 micromol h(-)(1) (mg of protein)(-)(1). When DMA(V) or arsenate was tested as a substrate, the K(m) was 20.9 x 10(-)(3) or 109 x 10(-)(3) M, respectively. The enzyme has an absolute requirement for GSH. Other thiols such as DTT or L-cysteine were inactive alone. At a pH below the physiological pH, GSH carried out this reduction, but this GSH reduction in the absence of the enzyme had little if any value at pH 7.4. When the K(m) values of rabbit liver arsenite methyltransferase (5.5 x 10(-)(6) M) and MMA(III) methyltransferase (9.2 x 10(-)(6)) were compared to that of MMA(V) reductase (2.16 x 10(-)(3) M), it can be concluded that MMA(V) reductase was the rate-limiting enzyme of inorganic arsenite biotransformation. MMA(V) reductase was also present in surgically removed human liver.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0893-228X
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1278-83
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Enzymatic reduction of arsenic compounds in mammalian systems: the rate-limiting enzyme of rabbit liver arsenic biotransformation is MMA(V) reductase.
pubmed:affiliation
Department of Molecular and Cellular Biology, The University of Arizona, Tucson, Arizona 85721-0106, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.