Abstract
Abstract The complete amino acid sequence of a type L Bence-Jones protein (an immunoglobulin λ light chain) has been determined, including the location of the disulfide bridges. λ light chains, like k light chains, are subject to extensive variation in primary structure in the NH2-terminal half, but the COOH-terminal portion appears to be invariant. When aligned to achieve maximum homology, about 40% of the amino acid residues are identical in the sequence of human k and λ chains. Genetic conservation of the main polypeptide chain conformation is reflected in the similar location of the disulfide bridges of k and λ chains and in the similarity in sequence around the half-cystine residues and throughout the entire molecule.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
