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重组2S白蛋白过敏原的体外稳定性

Stability of recombinant 2 S albumin allergens in vitro.

作者信息

Murtagh G J, Dumoulin M, Archer D B, Alcocer M J

机构信息

School of Life and Environmental Sciences, University of Nottingham, University Park, UK.

出版信息

Biochem Soc Trans. 2002 Nov;30(Pt 6):913-5. doi: 10.1042/bst0300913.

Abstract

Two well known 2 S albumins, Ber e 1 from brazil nut and sunflower 2 S albumin 8 (SFA-8), have been expressed in a eukaryotic system and purified. Analysis of recombinant versions of Ber e 1 and SFA-8 revealed them to be significantly more resistant to digestion by pepsin than BSA, and to be stable for up to 30 min in simulated gastric fluid. Unfolding monitored by CD indicated that both proteins were also very resistant to denaturation induced by heat and low pH. These results suggest that, although the ability of 2 S albumins to reach the circulatory system may be a prerequisite for the allergenicity of this group of proteins, stability is just one of a number of characteristics that provoke a selective immune response.

摘要

两种著名的2S白蛋白,来自巴西坚果的Ber e 1和向日葵2S白蛋白8(SFA - 8),已在真核系统中表达并纯化。对Ber e 1和SFA - 8的重组形式进行分析发现,它们对胃蛋白酶消化的抗性明显高于牛血清白蛋白(BSA),并且在模拟胃液中可稳定长达30分钟。通过圆二色光谱(CD)监测的去折叠表明,这两种蛋白质对热和低pH诱导的变性也具有很强的抗性。这些结果表明,尽管2S白蛋白进入循环系统的能力可能是这组蛋白质具有致敏性的一个先决条件,但稳定性只是引发选择性免疫反应的众多特征之一。

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