Huang T C, Zumft W G, Mortenson L E
J Bacteriol. 1973 Feb;113(2):884-90. doi: 10.1128/jb.113.2.884-890.1973.
Highly purified molybdoferredoxin, with a specific activity of 2.6 mumoles of acetylene reduced per min per mg of protein, was obtained from Clostridium pasteurianum. The protein at concentrations above 5 mg/ml exists in solution as a tetrameric complex with two subunits each of about 60,000 and 50,000 daltons. Two atoms of molybdenum are present per protein molecule of 220,000 daltons. The S(0) (20, w) was found to be 10.5. The tetramer dissociates into a dimer as demonstrated by a decreasing sedimentation coefficient with decreasing protein concentration. At low pH and ionic strength, further dissociation into the monomers is achieved. A method for the isolation of the protein subunits is described.
从巴氏梭菌中获得了高纯度的钼铁氧还蛋白，其比活性为每分钟每毫克蛋白质还原2.6微摩尔乙炔。蛋白质浓度高于5毫克/毫升时，在溶液中以四聚体复合物形式存在，由两个亚基组成，每个亚基分子量约为60,000和50,000道尔顿。每个220,000道尔顿的蛋白质分子中存在两个钼原子。发现沉降系数S(0) (20, w)为10.5。随着蛋白质浓度降低，沉降系数减小，表明四聚体解离为二聚体。在低pH和离子强度下，可进一步解离为单体。本文描述了一种分离蛋白质亚基的方法。
