Abstract
DURING the course of investigations into serum transaminase activities1, it was observed that α-ketobutyrate (2-oxobutanoate) underwent enzymic reduction in the presence of serum and reduced diphosphopyridine nucleotide. At the time this was interpreted as being due to serum lactic dehydrogenase because a commercial sample of crystalline lactic dehydrogenase prepared from rabbit skeletal muscle reduced α-ketobutyrate almost as readily as its normal substrate, pyruvate2. Further work, however, has indicated differences between the action of serum on α-ketobutyrate and its action on pyruvate.
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ROSALKI, S., WILKINSON, J. Reduction of α-Ketobutyrate by Human Serum. Nature 188, 1110–1111 (1960). https://doi.org/10.1038/1881110a0
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DOI: https://doi.org/10.1038/1881110a0
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