1575765

Source:http://linkedlifedata.com/resource/pubmed/id/1575765

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0014792, umls-concept:C0086168, umls-concept:C0086418, umls-concept:C1152039
pubmed:issue	8
pubmed:dateCreated	1992-6-1
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0101032
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase, http://linkedlifedata.com/resource/pubmed/chemical/Hydrocarbons, Brominated, http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes, http://linkedlifedata.com/resource/pubmed/chemical/methyl bromide
pubmed:status	MEDLINE
pubmed:month	Apr
pubmed:issn	0006-2952
pubmed:author	pubmed-author:BoltH MHM, pubmed-author:HallierEE, pubmed-author:PetelBB, pubmed-author:SchröderK RKR
pubmed:issnType	Print
pubmed:day	15
pubmed:volume	43
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	1671-4
pubmed:dateRevised	2004-11-17
pubmed:meshHeading	pubmed-meshheading:1575765-Erythrocytes, pubmed-meshheading:1575765-Glutathione Transferase, pubmed-meshheading:1575765-Humans, pubmed-meshheading:1575765-Hydrocarbons, Brominated, pubmed-meshheading:1575765-Isoelectric Point, pubmed-meshheading:1575765-Isoenzymes, pubmed-meshheading:1575765-Substrate Specificity
pubmed:year	1992
pubmed:articleTitle	Dissociation of a new glutathione S-transferase activity in human erythrocytes.
pubmed:affiliation	Institut für Arbeitsphysiologie an der Universität Dortmund, Germany.
pubmed:publicationType	Journal Article