Molecular cloning and bacterial expression of pheromone binding protein in the antennae ofHelicoverpa armigera(Hübner)

2004 ◽  
Vol 57 (1) ◽  
pp. 15-27 ◽  
Author(s):  
Gui Rong Wang ◽  
Kong Ming Wu ◽  
Yu Yuan Guo
Keyword(s):  
Molecular Cloning ◽  
Binding Protein ◽  
Bacterial Expression ◽  
Pheromone Binding Protein

scholarly journals Molecular cloning of an insect pheromone-binding protein

FEBS Letters ◽  
1989 ◽  
Vol 256 (1-2) ◽  
pp. 215-218 ◽  
Author(s):  
K. Raming ◽  
J. Krieger ◽  
H. Breer
Keyword(s):  
Molecular Cloning ◽  
Binding Protein ◽  
Insect Pheromone ◽  
Pheromone Binding Protein

scholarly journals Molecular cloning and bacterial expression of a general odorant-binding protein from the cabbage armyworm Mamestra brassicae

1998 ◽  
Vol 258 (2) ◽  
pp. 768-774 ◽  
Author(s):  
Martine Maibeche-Coisne ◽  
Sonia Longhi ◽  
Emmanuelle Jacquin-Joly ◽  
Carole Brunel ◽  
Marie-Pierre Egloff ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Binding Protein ◽  
Bacterial Expression ◽  
Odorant Binding Protein ◽  
Mamestra Brassicae ◽  
Odorant Binding

scholarly journals Responses of the Pheromone-Binding Protein of the Silk Moth Bombyx mori on a Graphene Biosensor Match Binding Constants in Solution

Sensors ◽  
2021 ◽  
Vol 21 (2) ◽  
pp. 499
Author(s):  
Caroline Bonazza ◽  
Jiao Zhu ◽  
Roger Hasler ◽  
Rosa Mastrogiacomo ◽  
Paolo Pelosi ◽  
...  
Keyword(s):  
Bombyx Mori ◽  
Binding Protein ◽  
Binding Constants ◽  
Isoamyl Acetate ◽  
The Other ◽  
Oxide Surface ◽  
Binding Assays ◽  
Pheromone Binding Protein ◽  
Silk Moth ◽  
Good Agreement

An electronic biosensor for odors was assembled by immobilizing the silk moth Bombyx mori pheromone binding protein (BmorPBP1) on a reduced graphene oxide surface of a field-effect transistor. At physiological pH, the sensor detects the B. mori pheromones, bombykol and bombykal, with good affinity and specificity. Among the other odorants tested, only eugenol elicited a strong signal, while terpenoids and other odorants (linalool, geraniol, isoamyl acetate, and 2-isobutyl-3-methoxypyrazine) produced only very weak responses. Parallel binding assays were performed with the same protein and the same ligands, using the common fluorescence approach adopted for similar proteins. The results are in good agreement with the sensor’s responses: bombykol and bombykal, together with eugenol, proved to be strong ligands, while the other compounds showed only poor affinity. When tested at pH 4, the protein failed to bind bombykol both in solution and when immobilized on the sensor. This result further indicates that the BmorPBP1 retains its full activity when immobilized on a surface, including the conformational change observed in acidic conditions. The good agreement between fluorescence assays and sensor responses suggests that ligand-binding assays in solution can be used to screen mutants of a binding protein when selecting the best form to be immobilized on a biosensor.

scholarly journals Molecular cloning of porcine soluble angiotensin-binding protein.

1992 ◽  
Vol 267 (25) ◽  
pp. 18067-18072
Author(s):  
N Sugiura ◽  
H Hagiwara ◽  
S Hirose
Keyword(s):  
Molecular Cloning ◽  
Binding Protein
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