0000000000732472
AUTHOR
Lucie Moitrier
[Fri-P2-105] Deciphering the ligand binding properties of the mouse odorant-binding protein OBP5 from Mus musculus
International audience; Odorant-binding proteins (OBPs) are abundant soluble proteins secreted in the nasal mucus of a variety of species which are believed to be involved in the transport of odorants towards olfactory receptors. In this study, we report the functional characterization of mouse OBP5 (mOBP5). mOBP5 was recombinantly expressed as a hexahistidine-tagged protein in bacteria and purified by metal affinity. Oligomeric state and secondary structure composition of mOBP5 was investigated using gel filtration and circular dichroism spectroscopy. Fluorescent experiments revealed that mOBP5 interacts with the fluorescent probe N-phenyl naphthylamine (NPN) with a micromolar affinity. Co…
The role of Odorant-Binding Proteins in nutrition under the control of microbiota
Two sexually dimorphic Odorant binding proteins are affected by microbiota
Strategy for recombinant expression of soluble functional N-terminal domain of human sweet taste receptor produced in Escherichia coli
International audience