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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
|
pubmed:dateCreated |
1986-8-20
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pubmed:abstractText |
As a step towards the cloning of the gene for fumarylacetoacetate hydrolase (FAH), we have purified the FAH mRNA from rat liver by specific immunoadsorption of polysomes. The relative abundance of this mRNA has been estimated to be 0.14%. The major in vitro translation product of the purified mRNA preparation is specifically precipitated by a rabbit anti-rat FAH antiserum and it is, furthermore, undistinguishable by criteria of mass and charge from purified rat FAH.
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pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0829-8211
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
64
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
489-93
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3718716-Amino Acid Metabolism, Inborn Errors,
pubmed-meshheading:3718716-Animals,
pubmed-meshheading:3718716-Humans,
pubmed-meshheading:3718716-Hydrolases,
pubmed-meshheading:3718716-Liver,
pubmed-meshheading:3718716-Polyribosomes,
pubmed-meshheading:3718716-Protein Biosynthesis,
pubmed-meshheading:3718716-RNA, Messenger,
pubmed-meshheading:3718716-Rats,
pubmed-meshheading:3718716-Reticulocytes,
pubmed-meshheading:3718716-Tyrosine
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pubmed:year |
1986
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pubmed:articleTitle |
Purification of mRNA coding for the enzyme deficient in hereditary tyrosinemia, fumarylacetoacetate hydrolase.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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