Purification and properties of a very high density lipoprotein from the hemolymph of the honeybee Apis mellifera.
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.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001516:Bees; D002241:Carbohydrates / Q000032:analysis; D006458:Hemolymph / Q000032:analysis; D005779:Immunodiffusion; D008055:Lipids / Q000032:analysis; D008075:Lipoproteins, HDL / Q000302:isolation & purification*; D008970:Molecular Weight
D000596:Amino Acids; D002241:Carbohydrates; D008055:Lipids; D008075:Lipoproteins, HDL; C026277:very high density lipoproteins