瓜果腐霉菌乙醛酸脱氢酶的分离与鉴定
Isolation and characterization of glyoxylate dehydrogenase from the fungus Sclerotium rolfsii.
作者信息
Balmforth A J, Thomson A
出版信息
Biochem J. 1984 Feb 15;218(1):113-8. doi: 10.1042/bj2180113.
Abstract
Glyoxylate dehydrogenase (glyoxylate:NAD+ oxidoreductase) was purified 600-fold in three steps from crude extracts of the fungus Sclerotium rolfsii (Corticium rolfsii Curzi). Two of the purification steps involved dye-affinity chromatography. The enzyme is a tetramer of Mr 250 000, with identical subunits of Mr 57 000. Inhibition studies suggest that there is one essential thiol group per active site.
摘要
从真菌齐整小核菌（罗耳阿太菌Curzi）的粗提物中分三步纯化乙醛酸脱氢酶（乙醛酸：NAD+氧化还原酶），纯化倍数达600倍。其中两步纯化涉及染料亲和色谱法。该酶是一种分子量为250000的四聚体，由分子量为57000的相同亚基组成。抑制研究表明，每个活性位点有一个必需的巯基。
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