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

• Published in: Analytical 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
• Language: English
• Published: San Diego, CA Elsevier Inc 01.02.1984; Elsevier
• Subjects: Analytical, structural and metabolic biochemistry; Apolipoprotein A-I; Apolipoprotein A-II; Apolipoproteins - blood; Apolipoproteins - isolation & purification; Biological and medical sciences; Electrophoresis, Polyacrylamide Gel; Fundamental and applied biological sciences. Psychology; Humans; Immunodiffusion; Immunoelectrophoresis, Two-Dimensional; Lipoproteins, HDL - isolation & purification; Lipoproteins, myelin; Proteins; Sodium Chloride; Urea; Immunological method
• ISSN: 0003-2697; 1096-0309
• DOI: 10.1016/0003-2697(84)90337-3

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.