1984
DOI: 10.1002/jnr.490120111
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A brain synaptic dopamine‐binding protein: Isolation and partial characterization

Abstract: A dopamine-binding protein (DABP) has been purified from the rat brain cortex to homogeneity. Solubilization of the DABP from the synaptosomal membranes (P2M) by cholic acid, subsequent agarose gel filtration of the cholic acid extract to separate phospholipids from the DABP, and lastly DA affinity chromatography successfully resulted in a purified DABP with approximately 0.006% yield in protein concentration and 0.03% yield in specific [3H]-DA binding. The specific [3H]-DA binding of the purified DABP was 117… Show more

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Cited by 8 publications
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