作者: Maurice Wikler , Koiti Titani , Tomotaka Shinoda , Frank W. Putnam
DOI: 10.1016/S0021-9258(18)96143-0
关键词: Trypsin 、 Molecule 、 Peptide sequence 、 Bence Jones protein 、 Chymotrypsin 、 Immunoglobulin light chain 、 Stereochemistry 、 Homology (biology) 、 Biology 、 Protein primary structure
摘要: Abstract The complete amino acid sequence of a type L Bence-Jones protein (an immunoglobulin λ light chain) has been determined, including the location disulfide bridges. chains, like k are subject to extensive variation in primary structure NH2-terminal half, but COOH-terminal portion appears be invariant. When aligned achieve maximum homology, about 40% residues identical human and chains. Genetic conservation main polypeptide chain conformation is reflected similar bridges chains similarity around half-cystine throughout entire molecule.