Kurosky A, Markel D E, Touchstone B, Peterson J W
J Infect Dis. 1976 Mar;133 Suppl:14-22. doi: 10.1093/infdis/133.supplement_1.s14.
Acrylamide gel electrophoresis demonstrated that the toxin of Vibrio cholerae is comprised of three polypeptide chains, alpha, beta, and gamma, of molecular weights 24,000, 9,700, and 9,700 daltons, respectively. Amino acid sequence analysis of intact toxin indicated a molecular composition of alpha gamma beta4. Acrylamide gel electrophoresis and sequence analysis confirmed that the natural toxoid (choleragenoid) is identical to the toxin beta-chain. The alpha- and gamma-chains of the toxin are disulfide-linked (fragment A) but are noncovalently bound to the beta-chains. About 50% of the primary structure of the N-terminal portion of the beta-chain has been identified and a small segment of the D-terminus has also been characterized. Twenty residues of the N-terminal portions of the alpha- and gamma-chains have been tentativly identified. The amino acid composition of the beta-chain was determined and compared to that of the natural toxoid.
丙烯酰胺凝胶电泳表明，霍乱弧菌毒素由三条多肽链组成，分别为α、β和γ链，分子量分别为24,000、9,700和9,700道尔顿。完整毒素的氨基酸序列分析表明其分子组成为αγβ4。丙烯酰胺凝胶电泳和序列分析证实，天然类毒素（霍乱类毒素）与毒素β链相同。毒素的α链和γ链通过二硫键相连（A片段），但与β链非共价结合。β链N端部分约50%的一级结构已被确定，D端的一小段也已被表征。α链和γ链N端部分的20个残基已被初步鉴定。测定了β链的氨基酸组成并与天然类毒素进行了比较。
