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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1991-12-23
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pubmed:abstractText |
Effects of isoflurane on the DNase I activity in an isolated enzyme preparation and in the DNase I-globular (G) actin complex were investigated. DNase I, DNase I-G actin complex, and G actin were exposed to various (0.2-4.0 vol%) isoflurane concentrations for 180 min. Thereafter, DNase I activity was determined. DNase I activity was inhibited in relation to time and concentration of isoflurane exposure. At concentrations ranging from 0.2 to 1.0 vol% of isoflurane inactive DNase I was activated in the DNase I-G actin complex. The DNase I inhibitor G actin showed a reduced capability to inhibit DNase I following isoflurane exposure. Albumin can inhibit the DNase I inactivation possibly by competition in the reactions between DNase I/albumin and isoflurane. After exposure to isoflurane the absorption maximum of DNase I was identical with the absorption maximum of heat-denatured DNase I. The results suggest a mechanism by which isoflurane may affect DNA in an indirect way at concentrations to which the patient is exposed during clinical anesthesia.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0887-2082
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
129-35
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1941899-Actins,
pubmed-meshheading:1941899-Animals,
pubmed-meshheading:1941899-Buffers,
pubmed-meshheading:1941899-Cattle,
pubmed-meshheading:1941899-DNA Damage,
pubmed-meshheading:1941899-Deoxyribonuclease I,
pubmed-meshheading:1941899-Isoflurane,
pubmed-meshheading:1941899-Pancreas,
pubmed-meshheading:1941899-Protein Denaturation
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pubmed:year |
1991
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pubmed:articleTitle |
Effects of isoflurane on the DNase I activity in an isolated enzyme preparation and on the DNase I-G actin complex.
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pubmed:affiliation |
Department of Physiological Chemistry, University of Mainz, Federal Republic of Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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