Biewenga J, van Loghem E
Clin Chim Acta. 1978 Jan 2;82(1-2):201-4. doi: 10.1016/0009-8981(78)90045-1.
LDH-IgA complexes present in some human sera were purified by using affinity chromatography on 5'-AMP-Sepharose 4-B. The IgA component of the purified complexes was analysed in haemagglutination-inhibition tests. Antigenic determinants specific for alpha1 and alpha2 heavy chains and for kappa and lambda light chains were found. Earlier studies suggested that the IgA component is of kappa light chain type only. These different results are discussed. It is suggested that the LDH association site is located in the Fab fragment of the IgA component.
利用5'-AMP-琼脂糖4-B亲和层析法纯化了一些人血清中存在的乳酸脱氢酶-IgA复合物。在血凝抑制试验中分析了纯化复合物的IgA成分。发现了α1和α2重链以及κ和λ轻链特有的抗原决定簇。早期研究表明,IgA成分仅为κ轻链型。对这些不同结果进行了讨论。有人提出,乳酸脱氢酶结合位点位于IgA成分的Fab片段中。