Margaryan Armenak, Moaddel Ruin, Aldrich Jeffrey R, Tsuruda Jennifer M, Chen Angela M, Leal Walter S, Wainer Irving W
Gerontology Research Center, National Institutes in Aging, National Institutes of Health, Baltimore, MD 21224-6825, USA; USDA-ARS Chemicals Affecting Insect Behavior Laboratory Beltsville, MD 20705, USA.
Talanta. 2006 Nov 15;70(4):752-5. doi: 10.1016/j.talanta.2006.01.046. Epub 2006 Mar 3.
The pheromone-binding protein from the silkworm moth, Bombyx mori (BmorPBP) has been covalently bonded to a liquid chromatographic stationary phase. The resulting column was evaluated using radiolabeled bombykol and the immobilized protein retained its ability to bind this ligand. The data also demonstrate that the BmorPBP column was able to distinguish between four compounds, and rank them in their relative order of affinity for the protein from highest to lowest: bombykol>bombykal>1-hexadecanol>(Z,E)-5,7-dodecadien-1-ol, and that the immobilized BmorPBP retained its pH-dependent conformational mobility. The results of this study demonstrate that pheromone-binding protein from the silkworm moth, Bombyx mori and an odorant binding protein (OBP) obtained from the female mosquito Culex quinquefasciatoes have been immobilized on a silica support with retention of ligand-binding activity. The data indicate that proteins from non-mammalian organisms can be used to create liquid chromatography affinity columns.
