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Characterization of a putative pheromone biosynthesis-activating neuropeptide (PBAN) receptor from the pheromone gland of Heliothis peltigera
Year:
1999
Source of publication :
Invertebrate Neuroscience
Authors :
Altstein, Miriam
;
.
Ben-Aziz, Orna
;
.
Daniel, Shai
;
.
Gabay, Tal
;
.
Zeltser, Irina
;
.
Volume :
4
Co-Authors:
Altstein, M., Department of Entomology, ARO, Volcani Center, Bet Dagan 50250, Israel
Gabay, T., Department of Entomology, ARO, Volcani Center, Bet Dagan 50250, Israel
Ben-Aziz, O., Department of Entomology, ARO, Volcani Center, Bet Dagan 50250, Israel
Daniel, S.Shai, Department of Entomology, ARO, Volcani Center, Bet Dagan 50250, Israel
Zeltser, I., Department of Organic Chemistry, Hebrew Univ. of Jerusalem, Jerusalem 91904, Israel
Gilon, C., Department of Organic Chemistry, Hebrew Univ. of Jerusalem, Jerusalem 91904, Israel
Facilitators :
From page:
33
To page:
40
(
Total pages:
8
)
Abstract:
The binding of [3H]tyrosyl-PBAN28-33NH2 to pheromone gland membranes of the moth Heliothis peltigera was investigated. The study describes the development of a pheromone biosynthesis-activating neuropeptide (PBAN) radioreceptor assay and demonstrates the presence of a putative PBAN binding site on the pheromone gland. It also describes synthesis of a radioligand and optimization of binding conditions with respect to membrane preparation, number of gland equivalents, kinetics of ligand binding and composition of the binding solution. Binding was found to be optimal when membranes were freshly prepared from frozen glands, incubated at a concentration of one gland equivalent per reaction tube in the presence of 10 mM HCO3 - ions. Equilibrium of ligand binding was obtained after 20 min. Presence of other components such as NaCl, KCl or SH reagents did not have any effect on binding. Binding was found to be saturable, with a K(d) of 5.73 ± 1.05 x 10-6 M and a Bmax of 1.85 ± 0.22 nmol/mg protein. Binding was effectively displaced by unlabeled PBAN1-33NH2 and PBAN28-33NH2 with a K(i) of 4.3 ± 1.1 x 10-6 M and 4.9 ± 2.6 x 10-6 M, respectively.
Note:
Related Files :
Animal
Animals
animal tissue
biosynthesis
Female
Male
metabolism
pheromones
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More details
DOI :
Article number:
0
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
30675
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:56
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Scientific Publication
Characterization of a putative pheromone biosynthesis-activating neuropeptide (PBAN) receptor from the pheromone gland of Heliothis peltigera
4
Altstein, M., Department of Entomology, ARO, Volcani Center, Bet Dagan 50250, Israel
Gabay, T., Department of Entomology, ARO, Volcani Center, Bet Dagan 50250, Israel
Ben-Aziz, O., Department of Entomology, ARO, Volcani Center, Bet Dagan 50250, Israel
Daniel, S.Shai, Department of Entomology, ARO, Volcani Center, Bet Dagan 50250, Israel
Zeltser, I., Department of Organic Chemistry, Hebrew Univ. of Jerusalem, Jerusalem 91904, Israel
Gilon, C., Department of Organic Chemistry, Hebrew Univ. of Jerusalem, Jerusalem 91904, Israel
Characterization of a putative pheromone biosynthesis-activating neuropeptide (PBAN) receptor from the pheromone gland of Heliothis peltigera
The binding of [3H]tyrosyl-PBAN28-33NH2 to pheromone gland membranes of the moth Heliothis peltigera was investigated. The study describes the development of a pheromone biosynthesis-activating neuropeptide (PBAN) radioreceptor assay and demonstrates the presence of a putative PBAN binding site on the pheromone gland. It also describes synthesis of a radioligand and optimization of binding conditions with respect to membrane preparation, number of gland equivalents, kinetics of ligand binding and composition of the binding solution. Binding was found to be optimal when membranes were freshly prepared from frozen glands, incubated at a concentration of one gland equivalent per reaction tube in the presence of 10 mM HCO3 - ions. Equilibrium of ligand binding was obtained after 20 min. Presence of other components such as NaCl, KCl or SH reagents did not have any effect on binding. Binding was found to be saturable, with a K(d) of 5.73 ± 1.05 x 10-6 M and a Bmax of 1.85 ± 0.22 nmol/mg protein. Binding was effectively displaced by unlabeled PBAN1-33NH2 and PBAN28-33NH2 with a K(i) of 4.3 ± 1.1 x 10-6 M and 4.9 ± 2.6 x 10-6 M, respectively.
Scientific Publication
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