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. 2000 Mar 5;269(1):155-9. doi: 10.1006/bbrc.2000.2115.
An antifungal protein, possessing a molecular weight of 28 kDa and an N-terminal sequence resembling chitinases, has been purified from the seeds of the field bean Dolichos lablab. The procedure involved extraction with aqueous buffer, affinity chromatography on Affi-gel blue gel, and ion exchange chromatography on CM-Sepharose. The protein, designated dolichin, exhibited antifungal activity against the fungi Fusarium oxysporum, Rhizoctonia solani, and Coprinus comatus. Dolichin was capable of inhibiting human immunodeficiency virus (HIV) reverse transcriptase and alpha- and beta-glucosidases which are glycohydrolases implicated in HIV infection. It had very low ribonuclease and cell-free translation-inhibitory activities.
从长豇豆种子中纯化出一种抗真菌蛋白,其分子量为28 kDa,N端序列与几丁质酶相似。该纯化过程包括用水性缓冲液提取、在Affi - gel蓝凝胶上进行亲和层析以及在CM - 琼脂糖凝胶上进行离子交换层析。这种名为多利钦的蛋白对尖孢镰刀菌、立枯丝核菌和毛头鬼伞等真菌具有抗真菌活性。多利钦能够抑制人类免疫缺陷病毒(HIV)逆转录酶以及α-和β-葡萄糖苷酶,这些糖苷水解酶与HIV感染有关。它的核糖核酸酶和无细胞翻译抑制活性非常低。