Schreier E, El Samei M B
Int J Pept Protein Res. 1979 Mar;13(3):337-40. doi: 10.1111/j.1399-3011.1979.tb01889.x.
An improved method for isolation of inorganic pyrophosphatase (EC 3.6.1.1) from Bacillus stearothermophilus is described. The enzyme was purified to more than 90% after two chromatographic steps. A molecular weight of 140,000 daltons was estimated by density gradient centrifugation. The isoelectric point was found to be 4.0.
本文描述了一种从嗜热脂肪芽孢杆菌中分离无机焦磷酸酶（EC 3.6.1.1）的改进方法。经过两步色谱分离后，该酶的纯度达到了90%以上。通过密度梯度离心法估计其分子量为140,000道尔顿。发现其等电点为4.0。
