温度诱导的血清淀粉样蛋白SAA解离

R.P. Linke
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引用次数: 4

摘要

血清淀粉样蛋白A (SAA)已被证明在高温下不稳定。在37℃及更低温度下,凝胶过滤测定的分子量约为180,000道尔顿,而在38℃以上,在空隙体积和大约12,000道尔顿的位置发现了额外的aa抗原活性。后者多肽的大小和免疫反应性与SAAL相似,因为它具有暴露于4°C的aa抗原决定因子(与SAA不同)。由于酶抑制剂PMSF不能阻止SAAL或类似分子的释放,因此提出了SAA的温度依赖解离。鉴于已知的发热后淀粉样蛋白的发生,体外aa抗原蛋白的大小和免疫反应性的变化可能表明体内类似的机制在aa型淀粉样变性的发生中很重要。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Temperature-Induced Dissociation of Serum Amyloid Protein SAA

Serum amyloid A protein (SAA) has been shown to be unstable at elevated temperatures. While in agreement with earlier reports, molecular weights of approximately 180,000 daltons were determined by gel filtration at 37°C and below, above 38°C additional AA-antigenic activity was found in the void volume and at the position of approximately 12,000 daltons. The latter polypeptide resembled in size and immunoreactivity SAAL in that it had AA-antigenic determinants exposed at 4°C (unlike SAA). Because the release of SAAL or a similar molecule could not be prevented by the enzyme inhibitor PMSF, a temperature-dependent dissociation of SAA is proposed.

In view of the known occurrence of amyloid following febrile conditions, the change in size and immunoreactivity of AA-antigenic proteins in vitro may indicate that a similar mechanism in vivo is important in the genesis of AA-type amyloidosis.

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