Purification and molecular cloning of human apolipoprotein F

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

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Apolipoproteins / genetics*
  • Apolipoproteins / isolation & purification*
  • Base Sequence
  • Blotting, Northern
  • Chromosome Mapping
  • Chromosomes, Human, Pair 12
  • Cloning, Molecular*
  • DNA, Complementary / chemistry
  • DNA, Complementary / isolation & purification
  • Glycosylation
  • Humans
  • Liver / chemistry
  • Molecular Sequence Data
  • Molecular Weight
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • RNA, Messenger / analysis
  • Trypsin / metabolism

Substances

  • Apolipoproteins
  • DNA, Complementary
  • Peptide Fragments
  • RNA, Messenger
  • apolipoprotein F
  • Trypsin

Associated data

  • GENBANK/L27050