Abstract
The colchicine-binding protein in the soluble fraction of rat brain was characterized biochemically and immunologically. On the basis of molecular size and charge, the tight binding of colchicine appeared to be the property of a single macromolecule. Colchicine-binding protein was purified from the soluble fraction of rat brain by the ammonium sulfate fractionation-DEAE chromatography method and also by precipitation with vinblastine sulfate. Both preparations interacted similarly with antibody but only the latter elicited a humoral immune response in rabbits. The possible significance and causes of the immunological discrepancy are discussed.
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