Purification and characterization of a novel phospholipid transfer protein from filamentous fungi

Int J Biochem. 1990;22(1):93-8. doi: 10.1016/0020-711x(90)90083-f.

Abstract

1. We have isolated from mycelia of Mucor mucedo, a filamentous fungus, a phospholipid transfer protein. 2. The purification steps were gel filtration, hydroxyapatite chromatography, blue affinity column and fast protein liquid chromatography on anion exchanger. 3. A purified protein was obtained with a molecular mass of 24 kDa and a pI of 5.05 and its N-terminal sequence was established. 4. This protein transfers phosphatidylinositol, as well as phosphatidylcholine and phosphatidylethanolamine.

MeSH terms

  • Amino Acid Sequence
  • Ammonium Sulfate
  • Carrier Proteins / isolation & purification*
  • Chemical Precipitation
  • Hot Temperature
  • Hydrogen-Ion Concentration
  • Isoelectric Point
  • Membrane Proteins / isolation & purification*
  • Molecular Sequence Data
  • Mucor / analysis*
  • Mucor / growth & development
  • Phospholipid Transfer Proteins*
  • Phospholipids / isolation & purification*

Substances

  • Carrier Proteins
  • Membrane Proteins
  • Phospholipid Transfer Proteins
  • Phospholipids
  • Ammonium Sulfate