Abstract
Proteins with molecular weight (MW) higher than 100 kD are present in the fibrils extracted from amyloid deposits of patient And (λ VI AL amyloidosis). These proteins (MW 135-140 kD) have a high content of glycine (21%) and can be proteolyzed by bacterial collagenase. Electron microscopy study demonstrates that collagenase induces a significant modification of the supramolecular organization of the AL amyloid fibrils.
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.
