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ISOLATION OF HYDROPHOBIC PROTEINS BINDING NEUROTRANSMITTER AMINOACIDS. GLUTAMATE RECEPTOR OF THE SHRIMP MUSCLE
Author(s) -
Plazas Sara Fiszer,
Robertis E. De
Publication year - 1974
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1974.tb12207.x
Subject(s) - chloroform , glutamate receptor , sephadex , glutamic acid , chromatography , biochemistry , glutamine , amino acid , chemistry , elution , receptor , enzyme
— –Muscle of shrimps ( Artemisia longinaris ) were extracted with chloroform‐methanol (2:1, v/v) and the proteolipids were separated by column chromatography on Sephadex LH‐20. Three peaks of protein were eluted with chloroform and one with chloroform‐methanol (4:1, v/v). Only the first peak eluted between 16 and 26 ml of chloroform showed binding for l ‐( 14 C]‐glutamate. The type of saturation curve obtained suggests the existence of single type of binding site. The saturation is reached at one mole of l ‐glutamate per 320,000 g protein and the purification achieved about 3200‐fold. The protein binding‐glutamate does not bind GABA, aspartate or glutamine. The binding of l ‐[ 14 C]‐glutamate was inhibited by dl ‐α ‐methyl glutamic acid and l ‐glutamic acid diethyl ester. The binding properties of this hydrophobic protein fraction suggest that it may represent the isolated glutamate receptor of the shrimp muscle.