Tsushima H, Mine H, Hoshika K, Kawakami Y, Hyodoh F, Ueki A
Department of Hygiene, Kawasaki Medical School, Kurashiki, Japan.
J Bacteriol. 1992 Jul;174(14):4807-10. doi: 10.1128/jb.174.14.4807-4810.1992.
A cysteine proteinase inhibitor was found in culture media of Candida albicans. Purification to homogeneity of the inhibitor was performed by carboxymethyl-papain-Sepharose affinity, DE-52 ion-exchange, and reverse-phase high performance liquid chromatographies. The purified inhibitor had an M(r) of 15 kDa and a pI of 4.9. It was more stable to heat and pH than most proteins. The N-terminal sequence of the first 30 residues demonstrated high similarity with that of human cystatin A. Thus, C. albicans cysteine proteinase inhibitor seems to belong to the cystatin superfamily. The inhibitor activity of the yeast cellular form was 4.0 times higher than that of the hyphal cellular form in 7-day culture media. It is suggested that the inhibitor has regulatory functions similar to those of its counterpart proteinases in the invasion of host cells.
在白色念珠菌的培养基中发现了一种半胱氨酸蛋白酶抑制剂。通过羧甲基木瓜蛋白酶-琼脂糖亲和色谱、DE-52离子交换色谱和反相高效液相色谱对该抑制剂进行了纯化，直至达到同质。纯化后的抑制剂分子量为15 kDa，等电点为4.9。与大多数蛋白质相比，它对热和pH更稳定。前30个残基的N端序列与人胱抑素A的N端序列高度相似。因此，白色念珠菌半胱氨酸蛋白酶抑制剂似乎属于胱抑素超家族。在7天的培养基中，酵母细胞形式的抑制剂活性比菌丝细胞形式的高4.0倍。提示该抑制剂在宿主细胞侵袭过程中具有与其对应蛋白酶相似的调节功能。
