Zikán J, Rozprimová L, Novotný J
Folia Microbiol (Praha). 1984;29(3):254-63. doi: 10.1007/BF02877317.
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.
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。