Abstract
Proteoglycans were extracted from articular discs with 4 M guanidinium chloride and separated by ion-exchange and gel-filtration chromatography into high molecular weight (Mr > 1000 000) species containing chondroitin sulphate (predominantly chondroitin 6-sulphate) and low molecular weight iduronic acid-rich dermatan sulphate proteoglycan(s). The chondroitin sulphate proteoglycan contained 21 % uronic acid and 17% protein. It gave rise on digestion with chondroitinase ABC to a protein core of apparent Mr 350 000 with an amino acid composition closely resembling that of the cartilage-type proteoglycans. Other characteristics shared with previously-described cartilage proteoglycans include the presence of keratan sulphate and the ability to aggregate with hyaluronic acid.
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.
