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人载脂蛋白F的纯化与分子克隆

Purification and molecular cloning of human apolipoprotein F.

作者信息

Day J R, Albers J J, Gilbert T L, Whitmore T E, McConathy W J, Wolfbauer G

机构信息

Department of Medicine, University of Washington, Seattle 98103.

出版信息

Biochem Biophys Res Commun. 1994 Sep 15;203(2):1146-51. doi: 10.1006/bbrc.1994.2302.

DOI:10.1006/bbrc.1994.2302
PMID:8093033
Abstract

In our effort to study proteins that are involved in high density lipoprotein metabolism, we have identified apolipoprotein F and isolated a full length cDNA clone. Apolipoprotein F, with an apparent molecular mass of 29 kilodaltons, was purified from human high density lipoproteins using a modified two dimensional electrophoresis procedure. The cDNA, with a size of 1735 base pairs, was cloned from a Hep G2 cDNA library. The cDNA encodes apolipoprotein F, which is composed of 162 amino acids, and predicts that apolipoprotein F is a proteolytic product of a larger protein. Northern blot analysis indicates that apolipoprotein F mRNA is detected only in liver for the tissues examined. The gene was mapped to human chromosome number 12 using a human/rodent somatic cell hybrid mapping panel.

摘要

在我们对参与高密度脂蛋白代谢的蛋白质的研究中,我们鉴定出了载脂蛋白F并分离出了一个全长cDNA克隆。载脂蛋白F的表观分子量为29千道尔顿,使用改良的二维电泳方法从人高密度脂蛋白中纯化得到。该cDNA大小为1735个碱基对,是从Hep G2 cDNA文库中克隆出来的。该cDNA编码由162个氨基酸组成的载脂蛋白F,并预测载脂蛋白F是一种较大蛋白质的蛋白水解产物。Northern印迹分析表明,在所检测的组织中,仅在肝脏中检测到载脂蛋白F mRNA。使用人/啮齿动物体细胞杂交定位板将该基因定位到人类第12号染色体上。

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