| pubmed-article:2351649 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2351649 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:2351649 | lifeskim:mentions | umls-concept:C0032105 | lld:lifeskim |
| pubmed-article:2351649 | lifeskim:mentions | umls-concept:C0028630 | lld:lifeskim |
| pubmed-article:2351649 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
| pubmed-article:2351649 | lifeskim:mentions | umls-concept:C0678226 | lld:lifeskim |
| pubmed-article:2351649 | lifeskim:mentions | umls-concept:C0052181 | lld:lifeskim |
| pubmed-article:2351649 | lifeskim:mentions | umls-concept:C0032529 | lld:lifeskim |
| pubmed-article:2351649 | lifeskim:mentions | umls-concept:C1706204 | lld:lifeskim |
| pubmed-article:2351649 | lifeskim:mentions | umls-concept:C1555721 | lld:lifeskim |
| pubmed-article:2351649 | pubmed:issue | 17 | lld:pubmed |
| pubmed-article:2351649 | pubmed:dateCreated | 1990-7-16 | lld:pubmed |
| pubmed-article:2351649 | pubmed:abstractText | Genetic polymorphism of human plasma apolipoprotein A-IV has been detected by isoelectric focusing techniques followed by immunoblotting. The molecular basis for this apoA-IV polymorphism has been elucidated. Analysis of the protein coding sequences of the apoA-IV alleles 1 and 2 revealed a single G to T substitution in the apoA-IV-2 allele. The point mutation, occurring in a region highly conserved among the mouse, rat, and human A-IV apolipoproteins, converts the glutamine at position 360 of the mature protein to a histidine. This amino acid substitution adds one positive charge unit to the apoA-IV-1 isoprotein (pI 4.97) thus creating the more basic apoA-IV-2 isoprotein (pI 5.02). Computer analysis of the apoA-IV-2 allele revealed that the single G to T substitution results in the loss of a BbvI and a Fnu4HI restriction enzyme site and in the formation of a new restriction site for the enzyme SfaNI. Protein primary and secondary structure predictions were largely unaffected by this amino acid exchange. These results on the structure of the apoA-IV-1 and apoA-IV-2 alleles suggest that the three other rare isoproteins (apoA-IV-0, apoA-IV-3, and apoA-IV-4) are also due to nucleotide and subsequent amino acid substitutions in the apoA-IV sequence. | lld:pubmed |
| pubmed-article:2351649 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2351649 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2351649 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2351649 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2351649 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2351649 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2351649 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2351649 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:2351649 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:2351649 | pubmed:author | pubmed-author:BrewerH BHBJr | lld:pubmed |
| pubmed-article:2351649 | pubmed:author | pubmed-author:LohsePP | lld:pubmed |
| pubmed-article:2351649 | pubmed:author | pubmed-author:RaderD JDJ | lld:pubmed |
| pubmed-article:2351649 | pubmed:author | pubmed-author:KindtM RMR | lld:pubmed |
| pubmed-article:2351649 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2351649 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:2351649 | pubmed:volume | 265 | lld:pubmed |
| pubmed-article:2351649 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2351649 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2351649 | pubmed:pagination | 10061-4 | lld:pubmed |
| pubmed-article:2351649 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:2351649 | pubmed:meshHeading | pubmed-meshheading:2351649-... | lld:pubmed |
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| pubmed-article:2351649 | pubmed:meshHeading | pubmed-meshheading:2351649-... | lld:pubmed |
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| pubmed-article:2351649 | pubmed:meshHeading | pubmed-meshheading:2351649-... | lld:pubmed |
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| pubmed-article:2351649 | pubmed:meshHeading | pubmed-meshheading:2351649-... | lld:pubmed |
| pubmed-article:2351649 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2351649 | pubmed:articleTitle | Genetic polymorphism of human plasma apolipoprotein A-IV is due to nucleotide substitutions in the apolipoprotein A-IV gene. | lld:pubmed |
| pubmed-article:2351649 | pubmed:affiliation | Molecular Disease Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892. | lld:pubmed |
| pubmed-article:2351649 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2351649 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:2351649 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:337 | entrezgene:pubmed | pubmed-article:2351649 | lld:entrezgene |
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