Physical, chemical, and immunochemical studies of apolipoprotein A-I from pigeon plasma high density lipoproteins

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题名:	Physical, chemical, and immunochemical studies of apolipoprotein A-I from pigeon plasma high density lipoproteins
作者:	Mao SJT;Downing MR;Kottke BA.
贡献者:	Department of Biotechnology
日期:	1980-10
上传时间:	2009-11-26 01:43:41 (UTC+0)
出版者:	Asia University
摘要:	Pigeon plasma high density lipoproteins (HDL) were isolated by ultracentrifugation between the densities of 1.063 and 1.21 g/ml. Gel filtration of delipidated HDL in 5 M guanidine-HCl on Sephadex G-150 yielded a major fraction which eluted at the same position as human apolipoprotein A-I isolated from HDL. In SDS-gel electrophoresis, the isolated apolipoprotein co-migrated with human apolipoprotein A-I with a molecular weight of approx. 28 000. The amino acid composition was similar to the apolipoprotein A-I isolated from human and hen plasma. The isolated apolipoprotein from pigeon plasma had therefore been designated as apolipoprotein A-I. As judged by circular dichroism (CD), the apolipoprotein A-I displayed a maximum mean residue ellipticity of approx. -3 000 at 222 nm while at concentrations greater than 0.2 mg/ml. Calculations of alpha-helicial content gave values of 85%. Lowering the concentration of apolipoprotein A-I was found to concomitantly decrease the ellipticity (absolute value) suggesting that there was some conformational change when the apolipoprotein A-I concentration varied. The isolated pigeon apolipoprotein A-I was found bound to the phospholipid (dimyristoyl phosphatidylcholine) and there was no significant conformational change upon lipid binding as judged by CD. Under the same experimental conditions, human apolipoprotein A-I exhibited a drastic conformational change by increasing its helicity in the presence of phospholipid. The helical content of human apolipoprotein A-I was increased from 48 to 85%. This finding suggests that the apolipoprotein may not necessarily increase its helical content during lipid binding. Moreover, immunochemical studies showed that rabbit antiserum prepared against pigeon apolipoprotein A-I could partially react with human apolipoprotein A-I determined by quantitative radioimmunoassay.
關聯:	Biochemica et Biophysica Acta 620(1):100-10
显示于类别:	[生物科技學系] 期刊論文

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