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Title: L-( sup 3 H) glutamate binding to a membrane preparation from the optic lobe of the giant freshwater prawn Macrobrachium rosenbergii de Man

Abstract

Membrane preparation from the optic lobe of the giant freshwater prawn, Macrobrachium rosenbergii de Man, was examined for the presence of specific L-({sup 3}H) glutamate binding. The optic lobes were isolated from live animals. The tissue was homogenized and the membrane fraction isolated by differential centrifugation. The membrane suspension was incubated with 10-1,000 nM of L-({sup 3}H) glutamate at 37{degree}C for 60 min. Nonspecific binding was determined by incubating the mixture with 100 {mu}M L-glutamate. L-({sup 3}H) glutamate specifically bound to the membrane fraction with a dissociation equilibrium constant (Kd) of 205 nM and maximum number of binding sites (Bmax) of 2.04 n mol/mg protein. By using LIGAND computerized program, the saturation isotherm binding pattern indicates a single type of binding. To determine the type of glutamate receptors, competitive inhibition and IC{sub 50} of several glutamate agonists and antagonists were determined. The study reveals a metabotropic type of binding site.

Authors:
; ; ;  [1]
  1. Mahidol Univ., Bangkok (Thailand) Mahidol Univ., Nakorn Pathom (Thailand)
Publication Date:
OSTI Identifier:
5857879
Resource Type:
Journal Article
Journal Name:
Life Sciences; (USA)
Additional Journal Information:
Journal Volume: 48:1; Journal ID: ISSN 0024-3205
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; BIOCHEMICAL REACTION KINETICS; L CODES; GLUTAMIC ACID; CELL MEMBRANES; CENTRIFUGATION; CRUSTACEANS; RECEPTORS; TRACER TECHNIQUES; TRITIUM COMPOUNDS; AMINO ACIDS; ANIMALS; AQUATIC ORGANISMS; ARTHROPODS; CARBOXYLIC ACIDS; CELL CONSTITUENTS; COMPUTER CODES; HYDROGEN COMPOUNDS; INVERTEBRATES; ISOTOPE APPLICATIONS; KINETICS; MEMBRANE PROTEINS; MEMBRANES; ORGANIC ACIDS; ORGANIC COMPOUNDS; PROTEINS; REACTION KINETICS; SEPARATION PROCESSES; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Pratumtan, P, Govitrapong, P, Withyachumnarnkul, B, and Poolsanguan, B. L-( sup 3 H) glutamate binding to a membrane preparation from the optic lobe of the giant freshwater prawn Macrobrachium rosenbergii de Man. United States: N. p., 1991. Web. doi:10.1016/0024-3205(91)90421-7.
Pratumtan, P, Govitrapong, P, Withyachumnarnkul, B, & Poolsanguan, B. L-( sup 3 H) glutamate binding to a membrane preparation from the optic lobe of the giant freshwater prawn Macrobrachium rosenbergii de Man. United States. doi:10.1016/0024-3205(91)90421-7.
Pratumtan, P, Govitrapong, P, Withyachumnarnkul, B, and Poolsanguan, B. Tue . "L-( sup 3 H) glutamate binding to a membrane preparation from the optic lobe of the giant freshwater prawn Macrobrachium rosenbergii de Man". United States. doi:10.1016/0024-3205(91)90421-7.
@article{osti_5857879,
title = {L-( sup 3 H) glutamate binding to a membrane preparation from the optic lobe of the giant freshwater prawn Macrobrachium rosenbergii de Man},
author = {Pratumtan, P and Govitrapong, P and Withyachumnarnkul, B and Poolsanguan, B},
abstractNote = {Membrane preparation from the optic lobe of the giant freshwater prawn, Macrobrachium rosenbergii de Man, was examined for the presence of specific L-({sup 3}H) glutamate binding. The optic lobes were isolated from live animals. The tissue was homogenized and the membrane fraction isolated by differential centrifugation. The membrane suspension was incubated with 10-1,000 nM of L-({sup 3}H) glutamate at 37{degree}C for 60 min. Nonspecific binding was determined by incubating the mixture with 100 {mu}M L-glutamate. L-({sup 3}H) glutamate specifically bound to the membrane fraction with a dissociation equilibrium constant (Kd) of 205 nM and maximum number of binding sites (Bmax) of 2.04 n mol/mg protein. By using LIGAND computerized program, the saturation isotherm binding pattern indicates a single type of binding. To determine the type of glutamate receptors, competitive inhibition and IC{sub 50} of several glutamate agonists and antagonists were determined. The study reveals a metabotropic type of binding site.},
doi = {10.1016/0024-3205(91)90421-7},
journal = {Life Sciences; (USA)},
issn = {0024-3205},
number = ,
volume = 48:1,
place = {United States},
year = {1991},
month = {1}
}