Clem L W, Leslie G A
Dev Comp Immunol. 1982 Spring;6(2):263-9. doi: 10.1016/s0145-305x(82)80009-8.
Light chains from antibodies to the streptococcal A-variant carbohydrate from individual nurse sharks were compared by peptide maps of tryptic digests and amino acid compositions. Although the amino acid compositions of the different chains were quite similar, considerable differences as well as similarities were demonstrable on peptide maps. The peptide maps were interpreted as indicating that shark L chains likely have constant and variable regions as seen in the immunoglobulins of higher animals. Furthermore the unique peptides characteristic of different L chains support the hypothesis that nurse sharks, as a species, possess a relatively large number of different L chain amino acid sequences which are compatible with antibody binding sites to the streptococcal antigen. Hence the repetoire of nurse shark antibody combining sites to this antigen appears to be quite extensive.
通过胰蛋白酶消化产物的肽图和氨基酸组成,对来自个体护士鲨的抗链球菌A变体碳水化合物抗体的轻链进行了比较。尽管不同轻链的氨基酸组成非常相似,但在肽图上仍可显示出相当大的差异以及相似之处。肽图被解释为表明鲨鱼轻链可能具有与高等动物免疫球蛋白中所见的恒定区和可变区。此外,不同轻链特有的独特肽段支持了这样一种假设,即护士鲨作为一个物种,拥有相对大量不同的轻链氨基酸序列,这些序列与针对链球菌抗原的抗体结合位点兼容。因此,护士鲨针对该抗原的抗体结合位点库似乎相当广泛。