Warburton R J, Seybert D W
Department of Chemistry, Duquesne University, Pittsburgh, PA 15282.
Biochem Biophys Res Commun. 1988 Apr 15;152(1):177-83. doi: 10.1016/s0006-291x(88)80696-x.
Treatment of bovine adrenodoxin reductase with trypsin under conditions of limited proteolysis yields two major fragments of apparent molecular weights 30,500 and 20,200. The fragments, which have been partially purified by affinity chromatography to remove most of the intact adrenodoxin reductase, retain adrenodoxin-dependent NADPH cytochrome c reductase activity. Kinetic analyses yield Vmax and Km (adrenodoxin) values of 485 min-1 and 0.96 microM, respectively, at an ionic strength of 0.13 M in comparison to 1059 min-1 and 0.40 microM, respectively, for intact adrenodoxin reductase under the same conditions.
在有限蛋白水解条件下用胰蛋白酶处理牛肾上腺皮质铁氧化还原蛋白还原酶，产生两个表观分子量分别为30,500和20,200的主要片段。这些片段已通过亲和色谱法进行部分纯化以去除大部分完整的肾上腺皮质铁氧化还原蛋白还原酶，它们保留了依赖肾上腺皮质铁氧化还原蛋白的NADPH细胞色素c还原酶活性。动力学分析表明，在离子强度为0.13 M的条件下，其Vmax和Km（肾上腺皮质铁氧化还原蛋白）值分别为485 min-1和0.96 microM，而在相同条件下完整的肾上腺皮质铁氧化还原蛋白还原酶的Vmax和Km值分别为1059 min-1和0.40 microM。
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