Binding properties of a locust's chemosensory protein.
The chemosensory protein CSP-sg4 of the desert locust Schistocerca gregaria binds reversibly N-phenyl-1-naphthylamine in fluorescent-binding assays, with a dissociation constant of 4 microM. Upon binding to the protein, the emission peaks of the fluorescent probe undergo a marked blue shift, accompanied by an order of magnitude increase of the maximum intensity. The assay has also allowed the measurement of the affinity of CSP to other aromatic and aliphatic compounds. The binding capacity of this protein is unaffected by thermal treatments up to 100 degrees C for 20 min. The ligand-binding characteristics of chemosensory proteins may help in clarifying the role of this recently discovered class of soluble proteins in chemoreception.
Ban
Liping
L
Department of Entomology, China Agricultural University, Beijing, China.
Zhang
Long
L
Yan
Yuhua
Y
Pelosi
Paolo
P
D000818:Animals; D001667:Binding, Competitive; D002628:Chemoreceptor Cells / Q000502:physiology*; D006110:Grasshoppers / Q000502:physiology*; D019476:Insect Proteins / Q000378:metabolism*; D007700:Kinetics; D008024:Ligands; D011994:Recombinant Proteins / Q000378:metabolism; D013050:Spectrometry, Fluorescence
C435683:CSP-sg4 protein, Schistocerca gregaria; D019476:Insect Proteins; D008024:Ligands; D011994:Recombinant Proteins