Purification and properties of a very high density lipoprotein from the hemolymph of the honeybee Apis mellifera

Biochemistry. 1987 Apr 7;26(7):1885-9. doi: 10.1021/bi00381a015.

Abstract

A larval-specific very high density lipoprotein (VHDL) has been isolated from the hemolymph of the honeybee Apis mellifera. VHDL was isolated by a combination of density gradient ultracentrifugation and gel filtration. The purified protein is a dimer of Mr 160,000 apoproteins as shown by chemical cross-linking with dimethyl suberimidate. N-Terminal sequence analysis indicates that the two polypeptide chains are identical. The holoprotein contains 10% lipid by weight and 2.6% covalently bound carbohydrate. A native Mr 330,000 species was obtained by gel permeation chromatography. Antiserum directed against VHDL was used to show that VHDL is distinct from other hemolymph proteins and appears to constitute a novel lipoprotein of unknown function. However, the lipoprotein is present in high amounts in hemolymph only at the end of larval life, suggesting a potential role in lipid transport and/or storage protein metabolism during metamorphosis.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Animals
  • Bees*
  • Carbohydrates / analysis
  • Hemolymph / analysis
  • Immunodiffusion
  • Lipids / analysis
  • Lipoproteins, HDL / isolation & purification*
  • Molecular Weight

Substances

  • Amino Acids
  • Carbohydrates
  • Lipids
  • Lipoproteins, HDL
  • very high density lipoproteins