ISOLATION OF HYDROPHOBIC PROTEINS BINDING NEUROTRANSMITTER AMINOACIDS. GLUTAMATE RECEPTOR OF THE SHRIMP MUSCLE |
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Authors: | Sara Fiszer de Plazas E De Robertis |
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Institution: | Institute de Biologia Celular. Facultad de Medicina, Universidad de Buenos Aires, Paraguay 2155, Buenos Aires, Argentina |
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Abstract: | Abstract— –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 -(14C]-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 -14C]-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. |
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