Characterization of apolipoproteins from chicken plasma

• Published in: Journal of Chromatography A 1990-07, Vol.512, p.203-212
• Main Authors: Brown, Eleanor M., Dower, Harold J.
• Format: Article
• Language: English
• Subjects: Analytical, structural and metabolic biochemistry; apolipoproteins; Biological and medical sciences; blood plasma; chickens; Fundamental and applied biological sciences. Psychology; high performance liquid chromatography; lipid transport; Lipoproteins, myelin; Proteins
• ISSN: 0021-9673
• DOI: 10.1016/S0021-9673(01)89486-3

Although functionally similar, the lipoprotein systems of birds and mammals differ in composition. the major apolipoproteins, apo A-I and apo B, are common to all vertebrates; however apo A-II and apo E, functionally important components of mammalian lipoproteins, are absent from chicken plasma. Chicken apo A-I and apo B have been characterized, and several minor apolipoprotein components have been observed in electrophoretic patterns of chicken lipoproteins. In this study a single density gradient ultracentrifugation was used to isolate and subfractionate chicken lipoproteins into density classes. Isolated lipoproteins were delipidated with hexane-sipopropanol (3:2). Apolipoproteins were then solubilized at pH 8.5 in 3 M guanidine hydrochloride and chromatographed on a 25 × 0.4 cm C 4 reversed-phase column using 0.1% trifluoroacetic acid in a gradient of acetonitrile in water. Molecular weights estimated by sodium dodecyl sulfate—polyacrylamide gel electrophoresis and amino acid compositions were compared with those of apolipoproteins from other species in a search for functional similarities. Similarities in composition between the major chicken apolipoprotein and several human apolipoproteins were observed.