Egorova O A, Avilova T V, Platonenkova L S, Egorov A M
Biokhimiia. 1981 Jun;46(6):1119-26.
NAD-dependent formate dehydrogenase was purified from a cell-free extract of methanol-consuming yeast Candida methylica, using chromatography on DEAE-cellulose and gel-filtration on Sephadex G-200. The enzyme is electrophoretically homogeneous, consists of two identical subunits with molecular weight of 46,000 and is active within the pH range of 6-9; the Km values for NAD and formate are 1 . 10(-4) and 1,3 . 10(-2) M, respectively. Formate dehydrogenase is inhibited by p-chloromercurybenzoate, iodoacetate, dithionitrobenzoate and azide.
依赖烟酰胺腺嘌呤二核苷酸（NAD）的甲酸脱氢酶是从消耗甲醇的酵母——甲基假丝酵母的无细胞提取物中纯化得到的，采用了二乙氨基乙基纤维素（DEAE - 纤维素）柱色谱法和葡聚糖凝胶G - 200凝胶过滤法。该酶在电泳上是均一的，由两个分子量为46,000的相同亚基组成，在pH 6 - 9范围内具有活性；NAD和甲酸的米氏常数（Km值）分别为1×10⁻⁴和1.3×10⁻²M。甲酸脱氢酶受到对氯汞苯甲酸、碘乙酸、二硫代硝基苯甲酸和叠氮化物的抑制。
