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  • 标题:Studies on the active center of D- and L-lactate dehydrogenases using oxamate-diaminohexyl-Sepharose affinity chromatography
  • 本地全文:下载
  • 作者:P Tuengler ; T N Stein ; G L Long
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1980
  • 卷号:77
  • 期号:10
  • 页码:5832-5836
  • DOI:10.1073/pnas.77.10.5832
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Vertebrate and invertebrate L-lactate dehydrogenases (L-lactate:NAD+ oxidoreductase, EC 1.1.1.27 ) are effectively bound to oxamate-diaminohexyl-Sepharose, whereas several D-lactate dehydrogenases (D-lactate:NAD+ oxidoreductase, EC 1.1.1.28 ) do not bind to the same Sepharose. One explanation for our findings is that the enzymes' substrate is oriented in a reversed manner in the active center of the D- and L-lactate dehydrogenases.
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