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Purification of transketolase from baker's yeast by an immunoadsorbent
N K Tikhomirova1, G A Kochetov
1A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
Abstract:
Baker's yeast transketolase has been purified by immunoaffinity chromatography on specific TK antibodies covalently linked to CNBr-agarose. Affinity chromatography allows a 480-fold purification of TK from yeast extracts and about 80% recovery of the original activity. The isolated enzyme has a specific activity of 12-60 U/mg and during polyacrylamide gel electrophoresis performed at pH 8.9 migrates as two protein bands possessing a transketolase activity which corresponds to two isoforms of the enzyme.