期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1971
卷号：68
期号：10
页码：2321-2324
DOI：10.1073/pnas.68.10.2321
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The sequence of the N-terminal ten amino acids of the unblocked light chains derived from the low molecular weight immunoglobulin of a dipnoid fish, the African lungfish (Protopterus aethiopicus), has been determined. A degree of sequence heterogeneity as extensive as that displayed by pooled mammalian light chains was encountered. The major N-terminal sequence of the amino acids of light chains from lungfish immunoglobins can be made homologous with that of various Elasmobranchean, Chondrostean, Avian, and Mammalian species if an internal deletion of two base triplets in the gene coding for light chains from lungfish immunoglobulins is assumed. The existence of a deletion and/or insertion mechanism may have profound biological significance, since it would be ideal for the introduction of variability into immunoglobulin chains without sacrificing certain integral features of the antibody molecule.
关键词：Protopterus aethiopicus ; 5.8 and 19S ; κ and λ chains
