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Differentation of Cl/sup -//Ca/sup 2 +/-dependent and sodium dependent /sup 3/H-glutamate binding to cortical membranes from rat brain by high energy radiation inactivation analysis

Abstract

The molecular weights of /sup 3/H-L-glutamate binding sites in the presence of chloride and calcium ions and in the presence of sodium ions were determined by the high energy irradiation technique. The molecular weight of sodium dependent /sup 3/H-L-glutamate binding sites, which has pharmacological specificities similar to the high-affinity uptake system for L-glutamate, was 670,000 daltons. The high-energy radiation inactivation study of chloride and calcium dependent and sodium independent /sup 3/H-L-glutamate binding is consonant with the idea that, this binding represent glutamate transport into resealed plasma membrane vesicles.
Publication Date:
Jan 01, 1986
Product Type:
Journal Article
Reference Number:
AIX-17-054717; EDB-86-145891
Resource Relation:
Journal Name: J. Neural Transm.; (Austria); Journal Volume: 65:2
Subject:
59 BASIC BIOLOGICAL SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; CELL MEMBRANES; MOLECULAR WEIGHT; RADIATION ABSORPTION ANALYSIS; GLUTAMIC ACID; RECEPTORS; CALCIUM; CEREBRAL CORTEX; CHLORIDES; INACTIVATION; RATS; SODIUM; TRACER TECHNIQUES; TRITIUM COMPOUNDS; ALKALI METALS; ALKALINE EARTH METALS; AMINO ACIDS; ANIMALS; BODY; BRAIN; CARBOXYLIC ACIDS; CELL CONSTITUENTS; CENTRAL NERVOUS SYSTEM; CEREBRUM; CHEMICAL ANALYSIS; CHLORINE COMPOUNDS; ELEMENTS; HALIDES; HALOGEN COMPOUNDS; ISOTOPE APPLICATIONS; LABELLED COMPOUNDS; MAMMALS; MEMBRANE PROTEINS; MEMBRANES; METALS; NERVOUS SYSTEM; NONDESTRUCTIVE ANALYSIS; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANS; PROTEINS; RODENTS; VERTEBRATES; 550200* - Biochemistry; 400104 - Spectral Procedures- (-1987)
OSTI ID:
5454711
Research Organizations:
Ferrosan A/S, Soeborg, Denmark; Sct. Hans Hospital, Roskilde, Denmark; Novo Industri A/S, Bagsvaerd, Denmark
Country of Origin:
Austria
Language:
English
Other Identifying Numbers:
Journal ID: CODEN: JNTMA
Submitting Site:
INIS
Size:
Pages: 93-101
Announcement Date:
Aug 01, 1986

Citation Formats

Honore, T, Drejer, J, Nielsen, M, and Braestrup, C. Differentation of Cl/sup -//Ca/sup 2 +/-dependent and sodium dependent /sup 3/H-glutamate binding to cortical membranes from rat brain by high energy radiation inactivation analysis. Austria: N. p., 1986. Web. doi:10.1007/BF01256485.
Honore, T, Drejer, J, Nielsen, M, & Braestrup, C. Differentation of Cl/sup -//Ca/sup 2 +/-dependent and sodium dependent /sup 3/H-glutamate binding to cortical membranes from rat brain by high energy radiation inactivation analysis. Austria. https://doi.org/10.1007/BF01256485
Honore, T, Drejer, J, Nielsen, M, and Braestrup, C. 1986. "Differentation of Cl/sup -//Ca/sup 2 +/-dependent and sodium dependent /sup 3/H-glutamate binding to cortical membranes from rat brain by high energy radiation inactivation analysis." Austria. https://doi.org/10.1007/BF01256485.
@misc{etde_5454711,
title = {Differentation of Cl/sup -//Ca/sup 2 +/-dependent and sodium dependent /sup 3/H-glutamate binding to cortical membranes from rat brain by high energy radiation inactivation analysis}
author = {Honore, T, Drejer, J, Nielsen, M, and Braestrup, C}
abstractNote = {The molecular weights of /sup 3/H-L-glutamate binding sites in the presence of chloride and calcium ions and in the presence of sodium ions were determined by the high energy irradiation technique. The molecular weight of sodium dependent /sup 3/H-L-glutamate binding sites, which has pharmacological specificities similar to the high-affinity uptake system for L-glutamate, was 670,000 daltons. The high-energy radiation inactivation study of chloride and calcium dependent and sodium independent /sup 3/H-L-glutamate binding is consonant with the idea that, this binding represent glutamate transport into resealed plasma membrane vesicles.}
doi = {10.1007/BF01256485}
journal = []
volume = {65:2}
journal type = {AC}
place = {Austria}
year = {1986}
month = {Jan}
}