A pheromone-binding protein (PBP) has been purified from the antennae of male Bombyx mori. It is a single polypeptide chain with a molecular weight of 16 kDa and an isoelectric point of 4.9. The PBP is present in the male and, to a minor extent, also in the female antennae, but not in other parts of the body. Strong crossreactivity has been observed with antibodies against the PBP of Antheraea polyphemus. Immunocytochemical localization indicates that the protein is concentrated in the sensillum lymph of sensilla trichodea
Recombinant Bombyx mori pheromone-binding protein (PBP), purified from an Escherichia coil expressio...
AbstractBackground: Insects use volatile organic molecules to communicate messages with remarkable s...
Pheromone-binding protein (PBP) and general odorant-binding proteins (GOBPs) were purified from the ...
A pheromone-binding protein (PBP) has been purified from the antennae of male Bombyx mori. It is a s...
Different odorant-binding proteins (OBPs) were isolated from total antennal homogenates of male and ...
The genome of the silkmoth Bombyx mori contains 44 genes encoding odorant-binding proteins (OBPs) an...
Pheromone-binding proteins are postulated to contribute to the exquisite specificity of the insect's...
SummaryInsect pheromone-binding proteins (PBPs) transport sex pheromones through the aqueous layer s...
The enormous capacity of the male silkmoth Bombyx mori in recognizing and discriminating bombykol an...
From an antennal library of Bombyx mori cDNA clones encoding different binding proteins have been is...
Pheromone-binding protein (PBP) and general odorant-binding proteins (GOBPs) were purified from the ...
0264-6021 (Print) Journal ArticleOdorant-binding proteins (OBPs) are thought to transport volatile c...
This paper reviews the characteristics of pheromone and odorant-binding proteins (OBP) in insects, w...
The Bombyx mori pheromone-binding protein (BmorPBP) is known to adopt two different conformations. T...
Male moths respond to conspecific female-released pheromones with remarkable sensitivity and specifi...
Recombinant Bombyx mori pheromone-binding protein (PBP), purified from an Escherichia coil expressio...
AbstractBackground: Insects use volatile organic molecules to communicate messages with remarkable s...
Pheromone-binding protein (PBP) and general odorant-binding proteins (GOBPs) were purified from the ...
A pheromone-binding protein (PBP) has been purified from the antennae of male Bombyx mori. It is a s...
Different odorant-binding proteins (OBPs) were isolated from total antennal homogenates of male and ...
The genome of the silkmoth Bombyx mori contains 44 genes encoding odorant-binding proteins (OBPs) an...
Pheromone-binding proteins are postulated to contribute to the exquisite specificity of the insect's...
SummaryInsect pheromone-binding proteins (PBPs) transport sex pheromones through the aqueous layer s...
The enormous capacity of the male silkmoth Bombyx mori in recognizing and discriminating bombykol an...
From an antennal library of Bombyx mori cDNA clones encoding different binding proteins have been is...
Pheromone-binding protein (PBP) and general odorant-binding proteins (GOBPs) were purified from the ...
0264-6021 (Print) Journal ArticleOdorant-binding proteins (OBPs) are thought to transport volatile c...
This paper reviews the characteristics of pheromone and odorant-binding proteins (OBP) in insects, w...
The Bombyx mori pheromone-binding protein (BmorPBP) is known to adopt two different conformations. T...
Male moths respond to conspecific female-released pheromones with remarkable sensitivity and specifi...
Recombinant Bombyx mori pheromone-binding protein (PBP), purified from an Escherichia coil expressio...
AbstractBackground: Insects use volatile organic molecules to communicate messages with remarkable s...
Pheromone-binding protein (PBP) and general odorant-binding proteins (GOBPs) were purified from the ...