Ye X Y, Ng T B
Department of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin.
J Protein Chem. 2001 Jul;20(5):353-9. doi: 10.1023/a:1012272518778.
A protein designated unguilin was isolated from seeds of the black-eyed pea (Vigna unguiculata). It possesses a molecular weight of 18 kDa and an N-terminal sequence resembling that of cyclophilins and the cyclophilin-like antifungal protein from mung beans, and was adsorbed on Affi-gel blue gel and CM-Sepharose. Unguilin exerted an antifungal effect toward fungi including Coprinus comatus, Mycosphaerella arachidicola, and Botrytis cinerea. In addition, unguilin was capable of inhibiting human immunodeficiency virus-1 reverse transcriptase and the glycohydrolases a- and beta-glucosidases which are involved in HIV infection. Unguilin was devoid of lectin and ribonuclease activities. It inhibited methyl-3H-thymidine uptake by mouse splenocytes and it weakly inhibited translation in a rabbit reticulocyte lysate system. Unguilin resembles mungin in some aspects, but differs from it in others.
从豇豆(Vigna unguiculata)种子中分离出一种名为unguilin的蛋白质。它的分子量为18 kDa,N端序列与亲环蛋白以及绿豆中的亲环蛋白样抗真菌蛋白相似,并且能吸附在Affi-凝胶蓝凝胶和CM-琼脂糖凝胶上。Unguilin对包括鸡腿菇、落花生尾孢菌和灰葡萄孢在内的真菌具有抗真菌作用。此外,unguilin能够抑制人类免疫缺陷病毒1型逆转录酶以及参与HIV感染的α-和β-糖苷水解酶。Unguilin没有凝集素和核糖核酸酶活性。它抑制小鼠脾细胞对甲基-3H-胸腺嘧啶的摄取,并且在兔网织红细胞裂解物系统中对翻译有微弱的抑制作用。Unguilin在某些方面与绿豆蛋白相似,但在其他方面又有所不同。