Glatz Z, Kovár J, Macholán L, Pec P
Biochem J. 1987 Mar 1;242(2):603-6. doi: 10.1042/bj2420603.
Diamine oxidase was prepared from pea (Pisum sativum) seedlings by a new purification procedure involving two h.p.l.c. steps. We studied the optical and electrochemical properties of the homogeneous enzyme and also analysed the hydrolysed protein by several methods. The data presented here suggest that the carbonyl cofactor of diamine oxidase is firmly bound pyrroloquinoline quinone.
通过一种涉及两步高效液相色谱的新纯化程序,从豌豆(Pisum sativum)幼苗中制备了二胺氧化酶。我们研究了该纯酶的光学和电化学性质,并通过多种方法分析了水解蛋白。本文给出的数据表明,二胺氧化酶的羰基辅因子是牢固结合的吡咯喹啉醌。