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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1993-2-26
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pubmed:databankReference |
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pubmed:abstractText |
Porcine lipoprotein lipase (LPL) cDNA has been cloned and sequenced. The deduced amino acid sequence shows a high degree of identity to LPL from other species, and contains the Ser/His/Asp triade characteristic of serine proteases and esterases. A repetitive element is present in the 3'-untranslated region of the cDNA. A partial cDNA covering the coding region of LPL detects three restriction fragment length polymorphisms with HindIII. This represents the first marker assigned to porcine chromosome 14.
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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:issn |
0268-9146
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
517-22
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1362860-Alleles,
pubmed-meshheading:1362860-Animals,
pubmed-meshheading:1362860-Chromosome Mapping,
pubmed-meshheading:1362860-Cloning, Molecular,
pubmed-meshheading:1362860-DNA,
pubmed-meshheading:1362860-Female,
pubmed-meshheading:1362860-Lipoprotein Lipase,
pubmed-meshheading:1362860-Male,
pubmed-meshheading:1362860-Pedigree,
pubmed-meshheading:1362860-Polymorphism, Restriction Fragment Length,
pubmed-meshheading:1362860-Swine
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pubmed:year |
1992
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pubmed:articleTitle |
Isolation and sequencing of porcine lipoprotein lipase cDNA and its use in multiallelic restriction fragment length polymorphism detection.
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pubmed:affiliation |
Department of Biochemistry, Norwegian College of Veterinary Medicine, Oslo.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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