Argiopinin-binding proteins from the membrane of the bull cerebral cortex

The 40 kDa argiopinin-binding glycoprotein has been isolated from the solubilised preparations of bovine cerebrum membranes by means of two-step biospecific chromatography on affinity sorbents with immobilized glutamate and argiopinins. This receptor component displays a specific L-[3H]glutamate bin...

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Bibliographic Details
Published inBioorganicheskaia khimiia Vol. 15; no. 8; p. 1022
Main Authors Volkova, T M, Avetisian, N A, Galkina, T G, Kudelin, A B, Makhmudova, E M, Solov'ev, M M, Tashmukhamedov, B A, Grishin, E V
Format Journal Article
LanguageRussian
Published Russia (Federation) 01.08.1989
Subjects
Amino Acids - metabolism
Animals
Carrier Proteins - isolation & purification
Carrier Proteins - metabolism
Cattle
Cerebral Cortex - metabolism
Chromatography, Affinity
Electrophoresis, Polyacrylamide Gel
Glutamates - metabolism
Glutamic Acid
Kinetics
Membrane Glycoproteins - metabolism
Oligopeptides - metabolism
Polyamines - metabolism
Receptors, Glutamate
Receptors, Neurotransmitter - metabolism
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Summary:The 40 kDa argiopinin-binding glycoprotein has been isolated from the solubilised preparations of bovine cerebrum membranes by means of two-step biospecific chromatography on affinity sorbents with immobilized glutamate and argiopinins. This receptor component displays a specific L-[3H]glutamate binding with Kd = 0.18 +/- +/- 0.019 mumole and Bmax = 43 +/- 4.5 nmole/mg. Amino acid analysis reveals it to be a member of integral membrane proteins.
ISSN:0132-3423