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水貂内毒素诱导的淀粉样变性中淀粉样纤维蛋白AA的一级结构。

The primary structure of amyloid fibril protein AA in endotoxin-induced amyloidosis of the mink.

作者信息

Waalen K, Sletten K, Husby G, Nordstoga K

出版信息

Eur J Biochem. 1980 Mar;104(2):407-12. doi: 10.1111/j.1432-1033.1980.tb04441.x.

Abstract

Two AA proteins were isolated from the same amyloid fibril preparation from the liver of a mink, in which amyloidosis had been induced by injections with endotoxin. The two proteins were of different size, one containing 53 amino acid residues and the other 64 residues. The amino acid sequence was otherwise found to be identical. Both proteins revealed pyrrolidone carboxylic acid as the N-terminal amino acid. Sequence homologies with protein AA from other species were very striking. However, no antigenic cross-reaction was seen between mink protein AA and antisera to protein AA from human, mouse or rabbit sources.

摘要

从一只水貂肝脏的同一份淀粉样纤维制剂中分离出了两种AA蛋白,该水貂的淀粉样变性是通过注射内毒素诱导产生的。这两种蛋白大小不同,一种含有53个氨基酸残基,另一种含有64个残基。除此之外,发现它们的氨基酸序列是相同的。两种蛋白的N端氨基酸均为吡咯烷酮羧酸。与其他物种的AA蛋白的序列同源性非常显著。然而,在水貂AA蛋白与来自人、小鼠或兔源的AA蛋白抗血清之间未观察到抗原交叉反应。

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