Simpson R J, Reid G E, Moritz R L, Morton C, Norton R S
Joint Protein Structure Laboratory, Ludwig Institute for Cancer Research, Royal Melbourne Hospital, Parkville, Victoria, Australia.
Eur J Biochem. 1990 Jun 20;190(2):319-28. doi: 10.1111/j.1432-1033.1990.tb15579.x.
The complete amino acid sequence of the cardiac stimulatory and haemolytic protein tenebrosin-C, from the Australian sea anemone Actinia tenebrosa, has been determined by Edman degradation of the intact molecule and fragments produced by treatment of the polypeptide chain with cyanogen bromide and enzymatic cleavage with endoproteinase Asp-N, thermolysin and trypsin. The molecule is a single-chain polypeptide consisting of 179 amino acid residues with a calculated molecular mass of 19,797 Da. Tenebrosin-C shows a high degree of amino acid sequence similarity (63%) with Stoichactis helianthus cytolysin III [Blumenthal, K. M. and Kem, W. R. (1983) J. Biol. Chem. 258, 5574-5581] and is identical to a partial sequence (90 residues) reported for equinatoxin, a cardiostimulatory and haemolytic protein isolated from the European sea anemone Actinia equina [Ferlan, I. and Jackson, K. (1983) Toxicon Suppl. 3, 141-144]. No amino acid sequence similarity was detected between tenebrosin-C and other protein sequences stored in available databases. The predicted secondary structure of tenebrosin-C suggests that it is a compact, highly structured molecule.
已通过对完整分子以及用溴化氰处理多肽链和用天冬氨酸内肽酶、嗜热菌蛋白酶和胰蛋白酶进行酶切产生的片段进行埃德曼降解，确定了来自澳大利亚海葵条纹海葵的心脏刺激和溶血蛋白tenebrosin-C的完整氨基酸序列。该分子是由179个氨基酸残基组成的单链多肽，计算分子量为19,797道尔顿。Tenebrosin-C与向日葵海葵溶细胞素III [布卢门撒尔，K. M. 和凯姆，W. R. (1983) 《生物化学杂志》258, 5574 - 5581] 显示出高度的氨基酸序列相似性 (63%)，并且与从欧洲海葵马氏海葵中分离出的一种心脏刺激和溶血蛋白海葵毒素报道的部分序列 (90个残基) 相同 [费兰，I. 和杰克逊，K. (1983) 《毒素学增刊》3, 141 - 144]。在tenebrosin-C与现有数据库中存储的其他蛋白质序列之间未检测到氨基酸序列相似性。Tenebrosin-C的预测二级结构表明它是一个紧密的、高度结构化的分子。
