Xu L L, Singh B K, Conn E E
Department of Biochemistry and Biophysics, University of California 95616.
Arch Biochem Biophys. 1988 Jun;263(2):256-63. doi: 10.1016/0003-9861(88)90634-0.
The hydroxynitrile lyase (EC 4.1.2.--) which catalyzes the dissociation of the cyanohydrins of acetone and 2-butanone has been isolated and purified from young seedlings of flax (Linum usitatissimum L.). The purification procedure involved precipitation with (NH4)2SO4, chromatofocusing, and chromatography on DEAE-cellulose, hydroxylapatite, Sephacryl 200, and Matrex Red A gel columns with a final recovery of 21%. Purification of 136-fold yielded an apparently homogeneous preparation that, in contrast to the lyases isolated from Prunus species, is not a flavoprotein. The subunit molecular weight of 42,000 was estimated by gel electrophoresis in the presence of sodium dodecyl sulfate. The native molecular weight of the enzyme was estimated by gel filtration (HPLC) to be 82,000. The enzyme has a narrow pH optimum around 5.5 and is highly stable at 4 degrees C.
已从亚麻（Linum usitatissimum L.）的幼苗中分离并纯化出催化丙酮和2-丁酮氰醇解离的羟腈裂解酶（EC 4.1.2.--）。纯化过程包括用硫酸铵沉淀、色谱聚焦以及在DEAE-纤维素、羟基磷灰石、Sephacryl 200和Matrex Red A凝胶柱上进行色谱分离，最终回收率为21%。136倍的纯化得到了一种明显均一的制剂，与从李属物种中分离出的裂解酶不同，它不是黄素蛋白。在十二烷基硫酸钠存在下通过凝胶电泳估计亚基分子量为42,000。通过凝胶过滤（HPLC）估计该酶的天然分子量为82,000。该酶在5.5左右有较窄的最适pH值，在4℃下高度稳定。
