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沟迎风海葵毒素III的氨基酸序列。

Amino acid sequence of toxin III from Anemonia sulcata.

作者信息

Bĕress L, Wunderer G, Wachter E

出版信息

Hoppe Seylers Z Physiol Chem. 1977 Aug;358(8):985-8. doi: 10.1515/bchm2.1977.358.2.985.

Abstract

Toxin III, the smallest toxin component of the poison of the sea anemone Anemonia sulcata, is a polypeptide with 27 amino acids. Its structure is stabilized by three disulfide bridges. The amino acid sequence was determined by solid-phase Edman degradation of the aminoethylated derivative. The peptide was coupled to the carrier, porous glass, by thiourea bridges between the alpha-amino group of arginine-1 and the epsilon-amino group of lysine-26 and the isothiocyanate groups of the carrier. Another fraction of the polypeptide was bound by an acid-amide condensation of the C-terminal valine-27 with the aminopropyl group of the carrier. The sequence of toxin III has no regions homologous to the 47-residue toxin II. Comparison with the known partial sequence of toxin I, which contains 46 amino acids (Wunderer, G. & Eulitz, M., in preparation) also fails to reveal homologies.

摘要

毒素III是沟迎风海葵毒液中最小的毒素成分,是一种含有27个氨基酸的多肽。其结构由三个二硫键稳定。氨基酸序列通过氨基乙基化衍生物的固相埃德曼降解法确定。该肽通过精氨酸-1的α-氨基与赖氨酸-26的ε-氨基之间的硫脲桥以及载体的异硫氰酸酯基团与载体多孔玻璃偶联。该多肽的另一部分通过C端缬氨酸-27与载体的氨丙基之间的酸酰胺缩合反应结合。毒素III的序列与47个残基的毒素II没有同源区域。与已知的含有46个氨基酸的毒素I的部分序列(温德雷尔,G.和尤利茨,M.,正在准备中)进行比较也未发现同源性。

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