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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Alternative splicing generates two different mRNA species for rat link protein.
TL;DR: The isolation of cDNA clones encoding the remainder of the rat link protein revealed the similarity in size between link 45 and the larger form of link protein (LP1) observed in other species appears fortuitous.
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Chick embryo fibroblasts produce two forms of hyaluronidase.
Roslyn W. Orkin,Bryan P. Toole +1 more
TL;DR: Data suggest that the secreted hyaluronidase differs from the cellular form in possessing additional sialic acid residues which endow the former with increased stability in the extracellular milieu.
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First Preclinical Imaging of Primary Cartilage Neoplasm and Its Local Recurrence Using 99mTc-NTP 15-5 Radiotracer
Elisabeth Miot-Noirault,François Gouin,Aurélien Vidal,Maryse Rapp,Jean Maublant,Serge Askienazy,Jean-Michel Chezal,Dominique Heymann,Françoise Rédini,Nicole Moins +9 more
TL;DR: These experimental results in 2 preclinical models of grade II chondrosarcoma bring forward data in favor of 99mTc-NTP 15-5 radiotracer for imaging primary growth of chondrobarcoma and its local recurrence after surgery.
Journal ArticleDOI
Failure of proteoglycans to form aggregates in morphologically normal aged human hip cartilage.
TL;DR: The results suggest that proteoglycan aggregation was diminished because of a defect in the core protein of the proteoglycans resulting in an impaired ability of these molecules to interact with hyaluronic acid.
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Biosynthesis of proteoglycans in organ cultures of developing kidney mesenchyme.
TL;DR: It is found that, as a response to induction, the differentiating mesenchyme begins to synthesize large size proteoglycans with an apparent molecular weight (MW) of 1 X 10(6) D.
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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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.