PURIFICATION AND MOLECULAR-CLONING OF HUMAN APOLIPOPROTEIN F+

Citation
Jr. Day et al., PURIFICATION AND MOLECULAR-CLONING OF HUMAN APOLIPOPROTEIN F+, Biochemical and biophysical research communications, 203(2), 1994, pp. 1146-1151
Citations number
10
Categorie Soggetti
Biology,Biophysics
ISSN journal
0006291X
Volume
203
Issue
2
Year of publication
1994
Pages
1146 - 1151
Database
ISI
SICI code
0006-291X(1994)203:2<1146:PAMOHA>2.0.ZU;2-0
Abstract
In our effort to study proteins that are involved in high density lipo protein 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 lipoprote ins using a modified two dimensional electrophoresis procedure. The cD NA, with a size of 1735 base pairs, was cloned from a Hep G2 cDNA libr ary. 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 apolipoprotei n 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.