Rybarska J, Konieczny L, Bobrzecka K, Laidler P
Immunol Lett. 1982 May;4(5):279-84. doi: 10.1016/0165-2478(82)90052-9.
Antibody-like molecules were formed by artificial recombination of proteolytic IgG fragments (Fab' with anti-SRBC activity, and Fc) and used for studies concerning the complement fixation. Such molecules, when composed of single Fab' bound to Fc fragment appeared inactive, while species containing two Fab' fragments revealed the hemolytic activity. The results were discussed and interpreted, assuming that the interaction of Fab domains with CH2 domains in the Fc fragment is a main structural effect influencing the binding of the complement.
通过蛋白水解IgG片段（具有抗SRBC活性的Fab'和Fc）的人工重组形成了抗体样分子，并用于补体固定相关研究。当这些分子由单个与Fc片段结合的Fab'组成时似乎无活性，而含有两个Fab'片段的分子则显示出溶血活性。在假设Fab结构域与Fc片段中CH2结构域的相互作用是影响补体结合的主要结构效应的前提下，对结果进行了讨论和解释。
