Blumenthal K M, Kem W R
J Biol Chem. 1983 May 10;258(9):5574-81.
The primary structure of Stoichactis helianthus cytolysin III has been determined by automated Edman degradation of the intact protein and of peptides derived therefrom by hydrolysis with trypsin and staphylococcal protease and by chemical cleavage with cyanogen bromide and o-iodosobenzoic acid. As a result of these studies, the positions of all 153 amino acid residues of toxin III have been unambiguously determined. Most regions of sequence were determined two times in different types of digests of the protein. A number of highly hydrophobic regions of sequence, which may be functionally significant, have been identified, including a region rich in tyrosine and tryptophan (residues 86-98). The secondary structure of toxin III has been predicted by Chou-Fasman analysis (Chou, P.Y., and Fasman, G.D. (1978) Annu. Rev. Biochem. 47, 251-276) of the primary structure. The predicted secondary structure contains 16% alpha-helix and 31% beta-structure.
通过对完整蛋白质以及用胰蛋白酶、葡萄球菌蛋白酶水解产生的肽段，还有用溴化氰和邻碘苯甲酸进行化学裂解产生的肽段进行自动埃德曼降解，确定了日光海葵细胞毒素III的一级结构。这些研究的结果明确确定了毒素III所有153个氨基酸残基的位置。大多数序列区域在蛋白质的不同类型消化物中被测定了两次。已鉴定出一些可能具有功能意义的高度疏水序列区域，包括富含酪氨酸和色氨酸的区域（第86 - 98位残基）。通过对一级结构进行周 - 法斯曼分析（Chou, P.Y., and Fasman, G.D. (1978) Annu. Rev. Biochem. 47, 251 - 276）预测了毒素III的二级结构。预测的二级结构包含16%的α - 螺旋和31%的β - 结构。
