Abstract
Highly purified J-chain was isolated from S-sulfonated human polymeric myeloma IgA by gel filtration and DEAE-cellulose chromatography, without using any dissociating agents. The purified J-chain was homogeneous upon immunoelectrophoresis and electrophoresis in agarose gel, alkaline-urea polyacrylamide gel, and sodium dodecyl sulfate polyacrylamide gel. The molecular weight of the J-chain, estimated by electrophoresis in sodium dodecyl sulfate polyacrylamide gel, was found to be 24 000 ± 1200 (S.D.). The J-chain dimerized in non-dissociating solvents, even in the presence of weak dissociating agents, such as 1 M propionic acid. During the isolation of the J-chain, two minor protein components which upon electrophoresis migrated, respectively, faster and slower than the J-chain itself were identified. These two components were antigenically unrelated to each other but both were clearly precipitated with anti-J-chain antisera, giving a reaction of partial identity to the J-chain. They were considered as two different fragments of J-chain, produced by some unknown protease(s).
Sign-in/Register to access full text options 
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.
