Abstract
A recombinant version of the receptor binding domain of rat α 1-macroglobulin (RBDv) consisting of residues 1319–1474 has been expressed in E. coli. Competition experiments with 125I-labelled methylamine treated human α 2-macroglobulin reveal that the α 1-macroglobulin-RBDv exhibit the same high affinity or the α 2-acroglobulin receptor as the entire 40 kDa light chain from rat α 1-macroglobulin. It is therefore concluded, that all determinants for receptor interaction reside in the C-terminal approx. 150 residues of the α-macroglobulin subunit.
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.
