一种不可解离的兔免疫球蛋白G-蛋白A复合物。

A non-dissociable rabbit IgG-protein a complex.

作者信息

Mota G, Galatiuc C, Sjöquist J, Ghetie V

出版信息

Ann Immunol (Paris). 1983 May-Jun;134C(3):331-40. doi: 10.1016/s0769-2625(83)80127-5.

Abstract

Glutaraldehyde treatment of rabbit IgG antibody complexed with protein A of Staphylococcus aureus (SpA) enabled the complex (IgG2-SpA1)2 to maintain its molecular weight unchanged and to become non-dissociable at low pH and in excess of IgG. The glutaraldehyde-treated (IgG2-SpA1)2 complex had the same half-life, complement-activating capacity and ability to interact with the Fc receptor as the non-treated complex. Moreover, the glutaraldehyde-treated complex had a stronger immunosuppressive effect on the synthesis of anti-sheep red blood cell antibody than either the non-complexed antibody or the IgG antibody complexed with SpA but untreated with glutaraldehyde.

摘要

用戊二醛处理与金黄色葡萄球菌A蛋白（SpA）复合的兔IgG抗体，能使复合物（IgG2-SpA1）2保持其分子量不变，并在低pH值和IgG过量的情况下不发生解离。经戊二醛处理的（IgG2-SpA1）2复合物与未处理的复合物具有相同的半衰期、补体激活能力以及与Fc受体相互作用的能力。此外，经戊二醛处理的复合物对抗绵羊红细胞抗体合成的免疫抑制作用比未复合的抗体或与SpA复合但未用戊二醛处理的IgG抗体更强。