葡萄球菌肠毒素A、B和C的近紫外圆二色性光谱分析

Leonard Spero
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引用次数: 3

摘要

对葡萄球菌肠毒素A、B和C在260 ~ 300 nm的近紫外CD光谱进行经验分解成高斯曲线。每个光谱都包含相同的六个成分,在几乎相同的波长上具有最大的椭圆度。然而,肠毒素A的旋转强度与肠毒素B和肠毒素c的旋转强度有显著差异。每个高斯曲线对应于芳香发色团的显著CD转变:两个苯丙氨酸带来自其1Lb转变(0-0和0 + 930 cm−1);从其1Lb跃迁(800 cm−1初级振动过程)中得到四条酪氨酸带,其中最弱的一条与苯丙氨酸带重叠;和一个1Lb色氨酸带。在碱性条件下,出现了以247 ~ 249 nm和295 ~ 298 nm为中心的酪氨酸CD条带。295 ~ 298 nm波段的低强度表明,中性肠毒素中的大部分酪氨酸CD是由埋藏残基贡献的。肠毒素A的色氨酸对CD的贡献呈阳性,而B和C的色氨酸对CD的贡献呈阴性。n -溴琥珀酰亚胺对a毒素的快速氧化和其他两种毒素中色氨酸残留对该试剂的不可用性也表明了不同的环境。二硫键在三种肠毒素中的环境明显不同。在肠毒素B和A易于还原的条件下,肠毒素C难以被巯基乙醇还原。肠毒素B二硫化物对其CD谱的贡献为正,强度约为9000°·cm2·dmol−1,集中在273 nm附近。原肠毒素A与还原肠毒素A之间的差异谱要小得多,似乎是构象起源。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Analysis of the near-ultraviolet circular dichroic spectra of staphylococcal enterotoxins A, B and C

The near-ultraviolet CD spectra from 260 to 300 nm of staphylococcal enterotoxins A, B and C were resolved empirically into Gaussian curves. Each spectrum contained the same six components with maximum ellipticities at virtually identical wavelengths. The rotatory strength of the bands of enterotoxin A, however, differed significantly from that of enterotoxins B and C. Each Gaussian curve was identified as corresponding to a prominent CD transition of an aromatic chromophore: two phenylalanine bands from its 1Lb transition (0-0 and 0 + 930 cm−1); four tyrosine bands from its 1Lb transition (the 800 cm−1 primary vibronic progression) with the weakest of these overlapping a phenylalanine band; and one 1Lb tryptophan band. At alkaline pH, tyrosylate CD bands arose, centered at 247–249 nm and at 295–298 nm. The low intensity of the 295–298-nm bands indicated that most of the tyrosine CD in the neutral enterotoxins was contributed by buried residues. The tryptophan contribution to the CD of enterotoxin A was positive, while that of B and C was negative. Also indicative of a different milieu was the ready oxidation of the A toxin by N-bromosuccinimide and the unavailability of the single tryptophan residue in the other two toxins to this reagent. The environment of the disulfide bond was markedly diverse in the three enterotoxins. Enterotoxin C was refractory to reduction by mercaptoethanol under conditions where enterotoxins B and A were readily reduced. The contribution of the disulfide of enterotoxin B to its CD spectrum was positive with an intensity of about 9000 deg · cm2 · dmol−1 and was centered near 273 nm. The difference spectrum between native and reduced enterotoxin A was much smaller and appeared to be conformational in origin.

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