Linked Life Data

6117446

Source:http://linkedlifedata.com/resource/pubmed/id/6117446

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1982-1-9
pubmed:abstractText
The stoichiometry of aminopyrine demethylation by rat liver microsomes is examined. The stoichiometry corresponds with combined oxidase/mono-oxygenase activities, i.e., 1 NADPH:1 oxygen:1 product (HCHO + H2O2). NADH synergism of NADPH-supported aminopyrine demethylation is accompanied by a synergism of NADPH-supported hydrogen peroxide formation and a severalfold increase in NADH consumption, further suggesting a relationship between the oxidase and mono-oxygenase reactions. During synergism the rate of cytochrome b5 oxidation is increased severalfold over that when the hemoprotein is reduced in the presence of either pyridine nucleotide alone, in agreement with earlier reports. This increased rate of cytochrome b5 reoxidation approximates the sum of the increased rates of oxidase plus mono-oxygenase reactions (expressed in terms of reducing equivalents), but is less than the increased rate of NADH oxidation (also in reducing equivalents). The suggestion is made that the NADPH-supported reaction opens pathways of metabolism in which electrons from NADH can participate.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0090-9556
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
461-5
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:articleTitle
Stoichiometry of aminopyrine demethylation with and without NADH synergism.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.