Suppr超能文献

γ1重链病的FOR蛋白以两种分子形式存在。

The gamma 1 heavy-chain disease FOR protein is present in two molecular forms.

作者信息

Zikán J, Rozprimová L, Novotný J

出版信息

Folia Microbiol (Praha). 1984;29(3):254-63. doi: 10.1007/BF02877317.

Abstract

Heavy chain disease proteins (FOR) were isolated from human plasma. These proteins were also detected immunochemically in the urine of the patient. The proteins were disulphide-linked Fc-like dimers with molar mass 64.2 kg/mol and sedimentation rate S020,W = 0.356 ps (3.56 S). Similar amounts of aspartic acid and pyroglutamic acid were found at the N-terminus. After cyanogen bromide cleavage of the FOR proteins, three peptides were isolated and their amino acid composition and partial amino acid sequence was determined. We suggest that two Fc-like proteins of similar sizes are present in the plasma: (1) the first with N-terminal aspartic acid corresponding to position 221 of gamma 1 EU chain and (2) the second with N-terminal pyroglutamic acid. The first protein and small amounts of related low-molar mass fragments found also in the plasma could be degradation products of the second protein. Evidence is given on structural differences between the FOR proteins and the corresponding portion of the gamma 1 EU chain.

摘要

重链病蛋白(FOR)从人血浆中分离得到。这些蛋白在患者尿液中也通过免疫化学方法检测到。这些蛋白是二硫键连接的Fc样二聚体,摩尔质量为64.2 kg/mol,沉降速率S020,W = 0.356 ps(3.56 S)。在N端发现了相似量的天冬氨酸和焦谷氨酸。对FOR蛋白进行溴化氰裂解后,分离出三个肽段,并测定了它们的氨基酸组成和部分氨基酸序列。我们认为血浆中存在两种大小相似的Fc样蛋白:(1)第一种N端为天冬氨酸,对应于γ1 EU链的第221位;(2)第二种N端为焦谷氨酸。第一种蛋白以及血浆中发现的少量相关低摩尔质量片段可能是第二种蛋白的降解产物。文中给出了FOR蛋白与γ1 EU链相应部分之间结构差异的证据。

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验