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.
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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.
View Article and Find Full Text PDFIsolation of argiopinin-binding protein from bovine brain.
J Protein Chem
June 1989
Shemyakin Institute of Bioorganic Chemistry, USSR Academy of Sciences, Moscow.
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