Isolation and characterization of proteoglycans from the swarm rat chondrosarcoma.
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Proteoglycan monomer (D1) and aggregate (A1) preparations were isolated from 4 M guanidinium chloride extracts of the Swarm rat chondrosarcoma and contained only small proteoglycan fragments, indicating that extensive enzymatic degradation had occurred.About:
This article is published in Journal of Biological Chemistry.The article was published on 1975-08-10 and is currently open access. It has received 543 citations till now. The article focuses on the topics: Proteoglycan & Benzamidine.read more
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Biosynthesis of Sulphated Macromolecules by Rabbit Lens Epithelium. I. Identification of the Major Macromolecules Synthesized by Lens Epithelial Cells In Vitro
J G Heathcote,Roslyn W. Orkin +1 more
TL;DR: Its presence in the culture medium was unanticipated but may be explained by the inability of these cultures to deposit a basement membrane when grown on a plastic surface, and its relationship to the lens epithelial basement membrane is the subject of the following paper.
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Proteoglycans in human laryngeal cartilage. Identification of proteoglycan types in successive cartilage extracts with particular reference to aggregating proteoglycans
Spyros S. Skandalis,Achilleas D. Theocharis,Demitrios H. Vynios,Dimitrios A. Theocharis,Nickoletta Papageorgakopoulou +4 more
TL;DR: The content, composition and structure of proteoglycans (PGs) in adult human laryngeal cartilage (HLC) were investigated by using two different extraction protocols and indicated that PBS extract contained very little amount of PGs.
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Age-Related Changes in Small Proteoglycans of Low buoyant Density of Human Articular Cartilage
TL;DR: Fragments of large monomers containing keratan sulfate and hyaluronic acid binding region are the major component of similar fractions from old cartilage.
Journal ArticleDOI
Ultrastructure of hydrated proteoglycans using a pulsed plasma source.
TL;DR: A wet-cell, which when used in concert with a pulsed plasma soft X-ray source, provides high contrast contact replicas of totally hydrated, unstained biological specimens, which exhibit good contrast and better than 30 nm spatial resolution when examined by conventional scanning electron microscope.
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Structure and composition of proteoglycans from human annulus fibrosus.
S. Inerot,I. Axelsson +1 more
TL;DR: Proteoglycans were extracted from ground human lumbar annuli fibrosi with 4M guanidinium chloride and purified by means of associative equilibrium density gradient centrifugation, and it was suggested that the proteoglyCans contain three regions: a chondroitin sulphate-rich region, a keratan sulphate -rich region and a region that binds to hyaluronic acid, thus allowing proteoglycan aggregates to be formed.
References
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Protein Measurement with the Folin Phenol Reagent
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The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
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TL;DR: It has been found possible to distinguish betweenHeparin, heparin derivatives, and other polyuronides of connective tissue by comparing the effect of chlorides on the color yield in both procedures by modifying Dische's carbazole reaction for uronic acid in the presence of borate.
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Enzymatic Methods for the Determination of Small Quantities of Isomeric Chondroitin Sulfates
TL;DR: Micromethods have been developed and 35S-labeled chondroitin sulfates A, B, and C in a given mixture have been precisely and rapidly determined by measuring radioactivity alone.