Slayter H S, Alexander R J, Steiner L A
Eur J Immunol. 1983 Feb;13(2):102-6. doi: 10.1002/eji.1830130204.
The complement protein C1q, isolated from bullfrog (Rana catesbeiana) serum, was found by electron microscopy to resemble human C1q; peripheral globular units, probably six in number, are connected by thin strands to a hollow stem-like central structure. The dimensions of frog and human C1q were also found to be very similar. These results are consistent with earlier observations that frog and human C1q are similar, although not identical, in overall size, subunit structure, amino acid composition, and functional properties. Evidently this protein, which binds to antigen-antibody complexes and to C1r and C1s, thereby forming a physical link between the immune and complement systems, has been highly conserved in evolution.
从牛蛙(牛蛙)血清中分离出的补体蛋白C1q,通过电子显微镜观察发现其与人类C1q相似;外周的球状结构,数量可能为六个,通过细链连接到一个中空的茎状中央结构。还发现青蛙和人类C1q的尺寸非常相似。这些结果与早期的观察结果一致,即青蛙和人类C1q在总体大小、亚基结构、氨基酸组成和功能特性方面相似但不完全相同。显然,这种与抗原-抗体复合物以及C1r和C1s结合,从而在免疫和补体系统之间形成物理连接的蛋白质,在进化过程中得到了高度保守。