Hadji-Azimi I
Immunology. 1971 Sep;21(3):463-73.
The anuran amphibian has been shown to produce two classes of antibodies to HGG, BSA and Hc. These antibodies were characterized by gel filtration on Sephadex G-200 as 19S' and 7S' immunoglobulins. In the course of immunization, antibody activity could be initially detected in the 19S' immunoglobulin fraction, followed by the appearance of the activity in the 7S' immunoglobulin fraction at a later stage of immunization. A switch-over from 19S' to 7S' activity was not observed. Both immunoglobulins were composed of heavy and light polypeptide chains. The 19S' protein had heavy chains with a molecular weight of 74,500, similar to human μ-chain (73,900). The 7S' protein differed from human IgG in respect to the molecular weight of its heavy chain which was shown to be 64,500. Light chains of both immunoglobulins of were found to have a molecular weight of 26,700, similar to human immunoglobulin light chains (25,000).
已证明无尾两栖动物能产生针对人γ球蛋白（HGG）、牛血清白蛋白（BSA）和血蓝蛋白（Hc）的两类抗体。这些抗体经葡聚糖凝胶G - 200凝胶过滤表征为“19S”和“7S”免疫球蛋白。在免疫过程中，抗体活性最初可在“19S”免疫球蛋白组分中检测到，随后在免疫后期“7S”免疫球蛋白组分中出现活性。未观察到从“19S”到“7S”活性的转换。两种免疫球蛋白均由重链和轻链多肽组成。“19S”蛋白的重链分子量为74,500，与人μ链（73,900）相似。“7S”蛋白的重链分子量为64,500，与人类IgG不同。两种免疫球蛋白的轻链分子量均为26,700，与人免疫球蛋白轻链（25,000）相似。
