Ye X Y, Wang H X, Ng T B
Department of Biochemistry, Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China.
Biochem Biophys Res Commun. 1999 Sep 16;263(1):130-4. doi: 10.1006/bbrc.1999.1166.
A protein, with a molecular weight of 20 kDa, and an N-terminal sequence analogous to those of thaumatin-like proteins (TLPs) and thaumatins, was first isolated from the legume of the French bean Phaseolus vulgaris cv Kentucky wonder using a simple procedure involving affinity and ion exchange chromatography. The protein was adsorbed on both CM-Sepharose and Affi-gel Blue Gel. It was the first leguminous TLP-like protein demonstrated to exert antifungal activity against Fusarium oxysporum, Pleurotus ostreatus, and Coprinus comatus but not against Rhizoctonia solani.
一种分子量为20千道尔顿的蛋白质，其N端序列与类甜蛋白（TLPs）和甜蛋白类似，最初是通过一种涉及亲和色谱和离子交换色谱的简单方法，从法国菜豆品种肯塔基奇观的豆科植物中分离出来的。该蛋白质能吸附在CM-琼脂糖凝胶和Affi-凝胶蓝凝胶上。它是首个被证明对尖孢镰刀菌、糙皮侧耳和平菇具有抗真菌活性，但对立枯丝核菌没有抗真菌活性的豆科类TLP样蛋白质。
