Ramazanova A S, Fil'kin S Iu, Starkov V G, Utkin Iu N
Bioorg Khim. 2011 May-Jun;37(3):374-85. doi: 10.1134/s1068162011030149.
Serine proteinases and Kunitz type inhibitors are widely represented in venoms of snakes from different genera. During the study of the venoms from snakes inhabiting Russia we have cloned cDNAs encoding new proteins belonging to these protein families. Thus, a new serine proteinase called nikobin was identified in the venom gland of Vipera nikolskii viper. By amino acid sequence deduced from the cDNA sequence, nikobin differs from serine proteinases identified in other snake species. Nikobin amino acid sequence contains 15 unique substitutions. This is the first serine proteinase of viper from Vipera genus for which a complete amino acid sequence established. The cDNA encoding Kunitz type inhibitor was also cloned. The deduced amino acid sequence of inhibitor is homologous to those of other proteins from that snakes of Vipera genus. However there are several unusual amino acid substitutions that might result in the change of biological activity of inhibitor.
丝氨酸蛋白酶和库尼茨型抑制剂在不同属的蛇毒中广泛存在。在对栖息于俄罗斯的蛇的毒液进行研究的过程中，我们克隆了编码属于这些蛋白质家族的新蛋白质的cDNA。因此，在极北蝰的毒腺中鉴定出一种名为尼科宾的新丝氨酸蛋白酶。根据cDNA序列推导的氨基酸序列，尼科宾与在其他蛇类物种中鉴定出的丝氨酸蛋白酶不同。尼科宾氨基酸序列包含15个独特的替换。这是极北蝰属蝰蛇中第一个确定了完整氨基酸序列的丝氨酸蛋白酶。编码库尼茨型抑制剂的cDNA也被克隆出来。推导的抑制剂氨基酸序列与极北蝰属其他蛇类的蛋白质同源。然而，存在几个不寻常的氨基酸替换，这可能导致抑制剂生物活性的改变。
