Ramseier H, Lindenmann J
Exp Cell Biol. 1977;45(1-2):101-17. doi: 10.1159/000162860.
The product of antigenic recognition (PAR) is an antigen-antibody complex with granulotactic activity. The following results support his conclusion. PAR generated by cell-bound or shed T-cell RS or the recognizing structure of T alloantisera and alloantigen can be destroyed by heating at 56 degrees C for 30 min, because of inactivation of a heat-labile component supplied by alloantigen. Recognizing partners of these complexes are heat-stable. They form PAR anew when alloantigen is added or upon confrontation with anti-RS serum. They are also capable of inducing anti-RS sera. PAR preparations composed of these recognizing structures and antibodies to them are heat-inactivated at much higher temperatures, because both partners of the complex are relatively heat-stable. Heat-labile PAR complexes (recognizing structures and alloantigen) pass anti-mouse immunoglobulin immunosorbent, but are retained specifically by alloantiserum (via alloantigen of the complex) or by anti-RS serum (via RS of the complex) bound to the column.
抗原识别产物（PAR）是一种具有粒细胞趋化活性的抗原-抗体复合物。以下结果支持了他的结论。由细胞结合或释放的T细胞识别结构（RS）或T同种异体抗血清和同种异体抗原的识别结构产生的PAR，可通过在56℃加热30分钟而被破坏，这是因为同种异体抗原提供的热不稳定成分失活。这些复合物的识别伙伴是热稳定的。当添加同种异体抗原或与抗RS血清接触时，它们会重新形成PAR。它们也能够诱导产生抗RS血清。由这些识别结构及其抗体组成的PAR制剂在高得多的温度下会发生热失活，因为复合物的两个伙伴都相对耐热。热不稳定的PAR复合物（识别结构和同种异体抗原）能通过抗小鼠免疫球蛋白免疫吸附柱，但会被结合在柱上的同种异体抗血清（通过复合物的同种异体抗原）或抗RS血清（通过复合物的RS）特异性保留。
