Characterization of proteoglycan and the proteoglycan-hyaluronic acid complex by electric birefringence
نویسندگان
چکیده
منابع مشابه
Characterization of proteoglycan and the proteoglycan--hyaluronic acid complex by electric birefringence.
An electric field causes partial alignment of macromolecules in a dilute solution. The accompanying changes in the solution birefringence offer a sensitive and quick means of monitoring the rates of particle orientation and hence the size of the solute molecules. Such measurements are reported for dilute solutions of proteoglycans in the absence and presence of added hyaluronic acid. The proteo...
متن کاملHyaluronic acid in cartilage and proteoglycan aggregation.
1. Dissociation of purified proteoglycan aggregates was shown to release an interacting component of buoyant density higher than that of the glycoprotein-link fraction of Hascall & Sajdera (1969). 2. This component, which produced an increase in hydrodynamic size of proteoglycans on gel chromatography, was isolated by ECTEOLA-cellulose ion-exchange chromatography and identified as hyaluronic ac...
متن کاملStudy of hyaluronic acid flexibility by electric birefringence.
Transient-electric-birefringence experiments were conducted on four samples of hyaluronic acid over the molecular-mass (M) range 5 X 10(4)-4 X 10(6) in dilute aqueous solution. The geometrical, optical and electrical characteristics were monitored via the rotary relaxation times, optical-polarizability antisotropies and electrical polarizabilities respectively. Each indicates the molecular conf...
متن کاملStructure of the complex between hyaluronic acid, the hyaluronic acid-binding region, and the link protein of proteoglycan aggregates from the swarm rat chondrosarcoma.
A complex consisting of the hyaluronic acid-binding region of proteoglycan molecules, the link protein, and hyaluronic acid was purified from trypsin digests of aggregates isolated from the Swarm rat chondrosarcoma. Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis showed that the molecular weights for the hyaluronic acid-binding region and the link protein were about 67,000 and 4...
متن کاملAffinity binding of the cartilage proteoglycan protein-keratan sulfate core to immobilized hyaluronic acid.
The protein-keratan sulfate core of bovine nasal cartilage proteoglycan was purified by affinity chromatography on a column of immobilized hyaluronic acid. The hyaluronic acid was immobilized by reaction with a hydrazido-alkyl derivative of Sepharose in the presence of borohydride. Proteoglycan was digested with chondroitinase ABC and the entire mixture was passed over a column of the Sepharose...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1978
ISSN: 0264-6021
DOI: 10.1042/bj1730237