Müller H P, Blobel H
Zentralbl Bakteriol Mikrobiol Hyg A Med Mikrobiol Infekt Parasitol. 1983 May;254(3):352-60.
A receptor for the Fc-component (FcR) of immunoglobulin (Ig) G was isolated from the cell-free supernatant of a Streptococcus dysgalactiae-culture by affinity chromatography on human IgG-sepharose. The single-step procedure yielded purified FcR with a specific activity of 1.1 x 10(6) U/mg protein. It had an estimated molecular weight of 78 000 dalton and an isoelectric point between pH 4.0 and 4.5. It was destroyed by pronase E and was sensitive to trypsin. Purified FcR gave strong single precipitin lines in the double immunodiffusion test with sera from human, horses, cattle, pigs, sheep, rabbits and guinea pigs. It also reacted with human IgG subgroup 3, differing from protein A of Staphylococcus aureus.
通过在人IgG - 琼脂糖上进行亲和层析，从停乳链球菌培养物的无细胞上清液中分离出免疫球蛋白G（IgG）的Fc成分受体（FcR）。该单步程序得到了比活性为1.1×10⁶U/mg蛋白质的纯化FcR。其估计分子量为78000道尔顿，等电点在pH 4.0至4.5之间。它可被链霉蛋白酶E破坏，对胰蛋白酶敏感。纯化的FcR在与人、马、牛、猪、羊、兔和豚鼠血清的双向免疫扩散试验中产生强单沉淀线。它也与人IgG亚群3反应，这与金黄色葡萄球菌的蛋白A不同。
