PURIFICATION AND MOLECULAR-CLONING OF HUMAN APOLIPOPROTEIN F+

被引:24
作者
DAY, JR
ALBERS, JJ
GILBERT, TL
WHITMORE, TE
MCCONATHY, WJ
WOLFBAUER, G
机构
[1] UNIV WASHINGTON,DEPT MED,NW LIPID RES LABS,SEATTLE,WA 98103
[2] ZYMOGENET CORP,SEATTLE,WA 98102
[3] UNIV N TEXAS,HLTH SCI CTR,DEPT MED,FT WORTH,TX 76107
[4] UNIV N TEXAS,HLTH SCI CTR,DEPT BIOCHEM,FT WORTH,TX 76107
关键词
D O I
10.1006/bbrc.1994.2302
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. 1994 Academic Press, Inc.
引用
收藏
页码:1146 / 1151
页数:6
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