Jr. Day et al., PURIFICATION AND MOLECULAR-CLONING OF HUMAN APOLIPOPROTEIN F+, Biochemical and biophysical research communications, 203(2), 1994, pp. 1146-1151
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.