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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1984-7-16
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pubmed:abstractText |
The apolipoprotein E2 ( apoE2 ) variant that possesses a cysteine substituted for an arginine at residue 158 in the amino acid sequence E2( Arg158 ----Cys) can be distinguished by sodium dodecyl sulfate-polyacrylamide gel electrophoresis from other forms of apoE, including E3 (the parent form), E4( Cys112 ----Arg), E2( Arg145 ----Cys), and E2( Lys146 ----Gln). The E2( Arg158 ----Cys) migrates as a distinctly separable band with a higher apparent molecular weight than the other forms. Chemical modification of apoE2 ( Arg158 ----Cys) with sulfhydryl reagents (2-bromoethyl)-trimethylammonium bromide or cysteamine, which convert cysteine to arginyl or lysyl analogues, respectively, abolishes the difference in apparent molecular weight and results in the co-electrophoresis of E2( Arg158 ----Cys) with other apoE forms. The mobilities of the other apoE variants are not affected by these modifications. These results suggest that the substitution site at residue 158 is a key location, important in modifying the behavior of apoE and in modulating its apparent molecular weight on sodium dodecyl sulfate-polyacrylamide gels. Furthermore, the technique used in this study may be very helpful in distinguishing specific mutant forms of apoE2 .
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoprotein E2,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins E,
http://linkedlifedata.com/resource/pubmed/chemical/Arginine,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteamine,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Reagents
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0022-2275
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
378-82
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:6726088-Amino Acid Sequence,
pubmed-meshheading:6726088-Apolipoprotein E2,
pubmed-meshheading:6726088-Apolipoproteins,
pubmed-meshheading:6726088-Apolipoproteins E,
pubmed-meshheading:6726088-Arginine,
pubmed-meshheading:6726088-Cysteamine,
pubmed-meshheading:6726088-Cysteine,
pubmed-meshheading:6726088-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:6726088-Genetic Variation,
pubmed-meshheading:6726088-Humans,
pubmed-meshheading:6726088-Isoelectric Focusing,
pubmed-meshheading:6726088-Molecular Weight,
pubmed-meshheading:6726088-Polymorphism, Genetic,
pubmed-meshheading:6726088-Protein Conformation,
pubmed-meshheading:6726088-Sulfhydryl Reagents
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pubmed:year |
1984
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pubmed:articleTitle |
Genetic polymorphism of apolipoprotein E: a variant form of apolipoprotein E2 distinguished by sodium dodecyl sulfate--polyacrylamide gel electrophoresis.
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pubmed:publicationType |
Journal Article
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