## Abstract Aging of articular cartilage results in accumulation of aggrecan fragments of various sizes that retain their ability to aggregate even though they may have relatively few glycosaminoglycan chains. Residual binding of partially degraded aggrecan may prevent binding of newly synthesized
The effect of link protein on the rheological properties of solutions of proteoglycan-hyaluronic acid aggregates
โ Scribed by Mitsugu Tomioka; Go Matsumura
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 679 KB
- Volume
- 27
- Category
- Article
- ISSN
- 0144-8617
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## Abstract Previous work has shown that alterations in proteoglycan aggregates are among the first changes detected with aging, disuse, and degeneration of articular cartilage, yet the cause or causes of these alterations remain unknown. To determine if differences in link protein concentration ca
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
## Abstract Proteoglycan aggregates isolated from normal bovine knee cartilage were larger than those from osteoarthritic cartilage of the same joints and appeared relatively more resistant to digestion with leech hyaluronidase. Incubation of proteoglycan subunits from the arthritic cartilage with
Thc @~ct.s ol'thc uddition qf'sodiiim hvulirronate segments ( s H A ) with d(ff2rent chain 1eng:lh.s on the vi.sc~oelasticiti 01' high molrculur I.t.eight sodiiim hyal~ironatc ( H A ) aqueoiis solutions wcrc studicd. Thc udditivc c$&~t.v of'.sHA &pcwdec.d on thc chain length o f s H A . Shorter sHA