Linked Life Data

4060148

Source:http://linkedlifedata.com/resource/pubmed/id/4060148

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-12-9
pubmed:abstractText
A rapid and reproducible in vitro test system was developed to measure the methemoglobin (MHb)-forming properties of various 8-aminoquinoline derivatives. Initial rates and extents of reaction were measured spectrophotometrically with either canine hemolysates from which ferrihemoglobin reductase was removed, or with purified human oxyhemoglobin (Hb). The results demonstrate that primaquine derivatives that can be oxidized to quinones or iminoquinones (5-hydroxy,6-desmethyl primaquine; 5-hydroxyprimaquine; 5,6-dihydroxy-8-aminoquinoline; and 5-hydroxy, 6-methoxy-8-aminoquinoline) are potent MHb-forming compounds. Studies on the extent of reaction in hemolysates and purified oxyhemoglobin suggest that the extent of MHb formation may be limited by the rate at which the corresponding iminoquinones or quinones arylate nucleophiles. The effects of glutathione, mannitol, ascorbate, and superoxide dismutase on the rate and extent of hemoglobin oxidation by 5,6-dihydroxy-8-aminoquinoline suggest that these compounds oxidize Hb similar to the mechanism known for dimethylaminophenol (DMAP), in which Hb oxidizes the quinoline to semiquinone radical and quinone species which are the oxidizing and arylating agents.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0041-008X
pubmed:author
pubmed:issnType
Print
pubmed:volume
81
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
192-202
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Structure-activity relationships of putative primaquine metabolites causing methemoglobin formation in canine hemolysates.
pubmed:publicationType
Journal Article, In Vitro