Sperti S, Montanaro L, Rambelli F, Stirpe F, Zamboni M
Ital J Biochem. 1986 Jul-Aug;35(4):266-71.
Gelonin, a plant protein which inactivates eukaryotic ribosomes, binds to zinc chelate Sepharose from which it is eluted with EDTA or histidine. After purification by metal chelate affinity chromatography, gelonin maintains the associated zinc-dependent proteinase activity previously described. In equilibrium dialysis about 4 moles of zinc bind per mole of gelonin with a dissociation constant of 0.96 mM. Ca2+ behaves as a mixed competitive and non-competitive inhibitor of the binding of zinc with Ki = 29 mM.
相思豆毒蛋白是一种能使真核核糖体失活的植物蛋白，它与锌螯合琼脂糖结合，可用乙二胺四乙酸（EDTA）或组氨酸将其从琼脂糖上洗脱下来。通过金属螯合亲和层析法纯化后，相思豆毒蛋白保持了先前所述的相关锌依赖性蛋白酶活性。在平衡透析中，每摩尔相思豆毒蛋白约结合4摩尔锌，解离常数为0.96毫摩尔。钙离子作为锌结合的混合竞争性和非竞争性抑制剂，其抑制常数（Ki）为29毫摩尔。
