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猪血清中过敏毒素去精氨酸ω-C5a的氨基酸序列和二硫键

Amino-acid sequence and disulfide linkages of the anaphylatoxin, des-Arg omega-C5a, from porcine serum.

作者信息

Zimmermann B, Vogt W

出版信息

Hoppe Seylers Z Physiol Chem. 1984 Feb;365(2):151-8. doi: 10.1515/bchm2.1984.365.1.151.

Abstract

The primary structure of the porcine complement-derived peptide, des-Arg omega-C5a, has been analysed. Des-Arg omega-C5a is the natural secondary product of the activation fragment of the fifth component of complement, C5a, and represents a classical anaphylatoxin. The elaborated amino-acid sequence confirms the structure of porcine C5a proposed earlier by Gerard and Hugli, with one exception. Further, by end-group determination and sequencing of the unreduced core of des-Arg omega-C5a the position of its three disulfide bridges has been determined, now allowing insight into the tertiary structure of des-Arg omega-C5a.

摘要

已对猪补体衍生肽去精氨酸ω-C5a的一级结构进行了分析。去精氨酸ω-C5a是补体第五成分C5a激活片段的天然二级产物,是一种典型的过敏毒素。详尽的氨基酸序列证实了杰勒德和胡格利之前提出的猪C5a结构,但有一个例外。此外,通过对去精氨酸ω-C5a未还原核心进行端基测定和测序,确定了其三个二硫键的位置,现在可以深入了解去精氨酸ω-C5a的三级结构。

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