Rodríguez-Ravelo Rodolfo, Restano-Cassulini Rita, Zamudio Fernando Z, Coronas Fredy I V, Espinosa-López Georgina, Possani Lourival D
Center for Mountain Development, Ministry of Science, Technology and, Environment, Limonar de Monte Roux, El Salvador Guantánamo, Cuba.
Department of Molecular Medicine and Bioprocesses, Biotechnology, Institute, National Autonomous University of Mexico, Avenida Universidad 2001, Colonia Chamilpa, Apartado Postal 510-3, Cuernavaca, Morelos 62210, Mexico.
Peptides. 2014 Mar;53:42-7. doi: 10.1016/j.peptides.2013.10.010. Epub 2013 Oct 25.
A proteomic analysis of the venom obtained from the Cuban scorpion Rhopalurus garridoi was performed. Venom was obtained by electrical stimulation, separated by high performance liquid chromatography, and the molecular masses of their 50 protein components were identified by mass spectrometry. A peptide of 3940 Da molecular mass was obtained in pure form and its primary structure determined. It contains 37 amino acid residues, including three disulfide bridges. Electrophysiological experiments showed that this peptide is capable of blocking reversibly K(+)-channels hKv1.1 with a Kd close to 1 μM, but is not effective against hKv1.4, hERG1 and EAG currents, at the same concentration. This is the first protein component ever isolated from this species of scorpion and was assigned the systematic number α-KTx 2.14.
对从古巴蝎子加氏棒尾蝎（Rhopalurus garridoi）获取的毒液进行了蛋白质组学分析。通过电刺激获取毒液，用高效液相色谱法进行分离，并用质谱法鉴定其50种蛋白质成分的分子量。获得了一种分子量为3940 Da的纯肽，并确定了其一级结构。它含有37个氨基酸残基，包括三个二硫键。电生理实验表明，该肽能够以接近1 μM的解离常数（Kd）可逆地阻断钾离子通道hKv1.1，但在相同浓度下对hKv1.4、hERG1和EAG电流无效。这是首次从这种蝎子中分离出的蛋白质成分，被赋予系统编号α-KTx 2.14。
