Linked Life Data

11305606

Source:http://linkedlifedata.com/resource/pubmed/id/11305606

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2001-4-17
pubmed:abstractText
The participation of reactive oxygen species (ROS) in virus inactivation by 1,9-dimethylmethylene blue (DMMB) phototreatment in stroma-free hemoglobin (SFH) was investigated with the use of scavengers, quenchers and enhancer. Virus (R17 bacteriophage) photoinactivation by either activated monomer or dimer DMMB was suppressed by sodium azide (singlet oxygen quencher) and promoted by the substitution of H2O for deuterium oxide (D2O), which is known to prolong the lifespan of singlet oxygen. There was no or little effect of mannitol (hydroxyl radical scavenger) and superoxide dismutase (superoxide scavenger) on the photoinactivation. Similar experiments were conducted to investigate the mechanism of methemoglobin (Met-Hb) formation by the activated monomer of DMMB. There was little effect of the singlet oxygen quencher, histidine, or the enhancer, D2O, on Met-Hb formation. However, rutin, which inhibits not only singlet oxygen but also other ROS, and mannitol supressed the formation of Met-Hb by activated monomer. The addition of superoxide dismutase (SOD) did not inhibit the formation. In contrast to the activity of the DMMB monomer, that of the dimer was inhibited by histidine and enhanced by D2O. The addition of neither mannitol nor SOD affected Met-Hb formation by activated dimer. These results collectively suggest that virus photoinactivation by the activated monomer and dimer of DMMB as well as Met-Hb formation by the activated dimer proceed via a singlet oxygen mediated pathway. In contrast, singlet oxygen may play a less important role in Met-Hb formation by the activated monomer.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0918-6158
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
418-21
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Involvement of reactive oxygen species in hemoglobin oxidation and virus inactivation by 1,9-dimethylmethylene blue phototreatment.
pubmed:affiliation
Hokkaido Red Cross Blood Center, Sapporo, Japan. hiraj@hokkaido.bc.jrc.or.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't