Hunneyball I M, Stanworth D R
Immunology. 1975 Nov;29(5):921-31.
Digestion of human IgG by a new lysine-specific protease, isolated from the basidiomycete Armillaria mellea, produced Fc and Fab fragments similar to those produced by papain digestion of the same molecule. Digestion appeared to be restricted to a single cleavage point within the hinge region of the IgG molecule. Myeloma proteins of IgG1, IgG3 and IgG4 subclasses were found to be digested at an extremely rapid rate whereas IgG2 myeloma proteins appeared to be resistant to digestion by this enzyme.
从担子菌蜜环菌中分离出的一种新型赖氨酸特异性蛋白酶对人IgG的消化作用产生了与木瓜蛋白酶消化同一分子时产生的类似Fc和Fab片段。消化作用似乎局限于IgG分子铰链区内的一个单一裂解点。发现IgG1、IgG3和IgG4亚类的骨髓瘤蛋白以极快的速度被消化，而IgG2骨髓瘤蛋白似乎对这种酶的消化具有抗性。
Zotero 插件