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Characterization of Lipophorin Receptor (LpR) Mediating the Binding of High Density Lipophorin (HDLp) in the Silkworm,Bombyx mori
Author(s) -
G. Ravikumar,
K. V. Vardhana,
H. Basavaraja
Publication year - 2011
Publication title -
journal of insect science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.551
H-Index - 49
ISSN - 1536-2442
DOI - 10.1673/031.011.15001
Subject(s) - bombyx mori , biology , bombycidae , receptor , polyclonal antibodies , microbiology and biotechnology , ligand (biochemistry) , recombinant dna , molecular mass , ldl receptor , biochemistry , antibody , gene , lipoprotein , genetics , enzyme , cholesterol
In an earlier report, we described the gene encoding a lipophorin receptor (LpR) of the silkworm, Bombyx mori L. (Lepidoptera: Bombycidae), and recombinant expression of the protein. The present study was performed to characterize the corresponding native Bm LpR and its binding characteristics. Polyclonal anti-LpR antibody prepared against the cloned receptor fragment from the cytoplasmic domain specifically detected the receptor. Through immunoblotting, ovary and brain membrane protein samples of Bm LpR have shown an apparent molecular mass of 105 kDa and 120 kDa under nonreducing and reducing conditions, respectively. Ligand binding of LpR supported the immunoblot results. It bound to high density lipophorin (HDLp) and has shown requirement of Ca 2 in binding. Further, a dose-dependent inhibition by EDTA was observed in receptor ligand binding. The characteristics of the Bm LpR protein confirm the properties of a ligand-receptor interaction similar to that of vertebrate low density lipoprotein receptor (LDLR).

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