Quantitation of apolipoprotein A-I in pooled human serum by single radial immunodiffusion and sodium dodecyl sulfate-polyacrylamide gel electrophoresis

Apolipoprotein A-I was released from human HDL particles by treatment with 8 m urea, and the free apolipoprotein exhibited identical antigenicity and the same low mobility as purified apolipoprotein A-I in electrophoresis. Treatment of serum with 8 m urea enabled quantitation of apolipoprotein A-I b...

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Published inAnalytical biochemistry Vol. 137; no. 1; pp. 1 - 7
Main Authors Sakai, Yasuo, Itakura, Koji, Kanada, Taira, Ebata, Nobuyoshi, Suga, Kazuo, Aikawa, Hideo, Nakamura, Kaname, Sata, Teizo
Format Journal Article
LanguageEnglish
Published San Diego, CA Elsevier Inc 01.02.1984
Elsevier
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Summary:Apolipoprotein A-I was released from human HDL particles by treatment with 8 m urea, and the free apolipoprotein exhibited identical antigenicity and the same low mobility as purified apolipoprotein A-I in electrophoresis. Treatment of serum with 8 m urea enabled quantitation of apolipoprotein A-I by single radial immunodiffusion assay, as judged by comparison with sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0003-2697
1096-0309
DOI:10.1016/0003-2697(84)90337-3