作者:S. B. ROSALKI、J. H. WILKINSON
DOI:10.1038/1881110a0
日期:1960.12
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.
在对血清转氨酶活性1进行调查的过程中,人们发现,在血清和还原二磷酸吡啶核苷酸存在的情况下,β-酮丁酸(2-氧代丁酸)会经历酶促还原。当时人们认为这是由于血清乳酸脱氢酶的作用,因为从兔骨骼肌制备的结晶乳酸脱氢酶的商业样品几乎像其正常底物丙酮酸2一样容易还原β-酮丁酸。然而,进一步的研究表明,血清对β-酮丁酸的作用与其对丙酮酸的作用有所不同。