Xu L L, Singh B K, Conn E E
Arch Biochem Biophys. 1986 Nov 1;250(2):322-8. doi: 10.1016/0003-9861(86)90733-2.
The enzyme mandelonitrile lyase (EC 4.1.2.10) which catalyzes the decomposition of the cyanohydrin of benzaldehyde has been isolated and purified to homogeneity from mature seeds of the California cherry (Prunus lyonii). The purification procedure involved chromatography on DEAE-cellulose and Con-A-Sepharose with a final recovery of 60% of enzyme activity. Purification of only 4.3-fold yielded a nearly homogeneous preparation. The absorption spectrum of this protein shows maxima at 278, 389, and 463 nm, indicative of its flavoprotein character. The native molecular weight for the lyase was found to be 50,000. The subunit molecular weight of 59,000 was estimated by gel electrophoresis in the presence of sodium dodecylsulfate. The isoelectric point was estimated to be 4.75. The enzyme has a narrow pH optimum around 5.5 and is highly stable at 4 degrees C.
扁桃腈裂解酶（EC 4.1.2.10）可催化苯甲醛氰醇的分解，已从加州樱桃（Prunus lyonii）的成熟种子中分离并纯化至同质。纯化过程包括在DEAE-纤维素和伴刀豆球蛋白A-琼脂糖上进行色谱分离，最终酶活性回收率为60%。仅4.3倍的纯化就得到了几乎同质的制剂。该蛋白质的吸收光谱在278、389和463 nm处有最大值，表明其黄素蛋白特性。发现裂解酶的天然分子量为50,000。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59,000。估计等电点为4.75。该酶在5.5左右有较窄的最适pH值，在4℃下高度稳定。
