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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1996-8-5
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pubmed:databankReference |
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pubmed:abstractText |
To study the expression of human xanthine dehydrogenase/oxidase (hXDH/XO), we cloned the cDNA covering its complete coding sequence and characterized it by translation in vitro in rabbit reticulocyte lysates and by transient expression in COS-1 cells. Two specific protein products with approximate molecular masses of 150 and 130 kDa were detected in both expression systems. These products are compatible with the molecular sizes of XDH/XO, and these peptides also showed immunoreactivity with polyclonal anti-hXDH antibodies. Significant XDH/XO enzyme activity (277 +/- 54 pmol/min per mg of protein) was measured in lysates of transfected COS cells, whereas in control transfections the activities were below the detection limit of our assay (0.2 pmol/min per mg of protein). The COS cells expressed the enzyme predominantly (89.8 +/- 0.3%) in the dehydrogenase form.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-1097132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-176939,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-1861983,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-1939050,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-1991828,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-2160073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-2981404,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-3163235,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-3529824,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-4342395,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-5665897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-6295573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-7575623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-7829092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-7852355,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-7876088,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-7956361,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-7989578,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-8135849,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-8224915,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-8248161,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8670112-8569197
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
315 ( Pt 1)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
235-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8670112-Amino Acid Sequence,
pubmed-meshheading:8670112-Animals,
pubmed-meshheading:8670112-Base Sequence,
pubmed-meshheading:8670112-Cloning, Molecular,
pubmed-meshheading:8670112-DNA, Complementary,
pubmed-meshheading:8670112-Gene Expression,
pubmed-meshheading:8670112-Humans,
pubmed-meshheading:8670112-Immunoblotting,
pubmed-meshheading:8670112-Molecular Sequence Data,
pubmed-meshheading:8670112-Protein Biosynthesis,
pubmed-meshheading:8670112-Rabbits,
pubmed-meshheading:8670112-Xanthine Dehydrogenase,
pubmed-meshheading:8670112-Xanthine Oxidase
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pubmed:year |
1996
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pubmed:articleTitle |
Cloning and expression in vitro of human xanthine dehydrogenase/oxidase.
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pubmed:affiliation |
Children's Hospital, University of Helsinki, Helsinki, Finland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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