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 cr...

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Bibliographic Details
Published in:Biochemistry (Easton) 1987-04, Vol.26 (7), p.1885-1889
Main Authors: Shipman, Barbara A, Ryan, Robert O, Schmidt, Justin O, Law, John H
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acids - analysis
Analytical, structural and metabolic biochemistry
Animals
APIS MELLIFERA
Bees
Biological and medical sciences
Carbohydrates - analysis
EPURATION
Fundamental and applied biological sciences. Psychology
HAEMOLYMPH
HEMOLINFA
Hemolymph - analysis
HEMOLYMPHE
Immunodiffusion
Lipids - analysis
LIPOPROTEINAS
LIPOPROTEINE
LIPOPROTEINS
Lipoproteins, HDL - isolation & purification
Lipoproteins, myelin
Molecular Weight
Proteins
PURIFICACION
PURIFICATION
SEPARACION
SEPARATING
SEPARATION
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Summary: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.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00381a015