Aggregation of Cartilage Proteoglycans: III. Characteristics of the Proteins Isolated from Trypsin Digests of Aggregates by D. Heinegård and others 2026-11-05
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By D. Heinegård and colleagues. Journal of Biological Chemistry 249(13), 4250–4256 (10 July 1974); DOI doi.org/10.1016/S0021-9258(19)42509-X
Abstract: enzymatic digestion of bovine nasal-cartilage aggregates, gel filtration and electrophoresis separate a core-protein-derived fraction from a link-protein fraction; both retain hyaluronic-acid binding.
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D. Heinegård 2026-11-05
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D. Heinegård investigated the molecular organization of cartilage proteoglycans. A 1974 study with colleagues dissected large proteoglycan assemblies using controlled proteolysis, gel filtration and gel electrophoresis.[ref]
Digestion yielded a fraction derived from the proteoglycan core protein and a distinct linking protein fraction. Both retained binding to hyaluronic acid. Separating components while testing which interaction survives is a useful way to infer how a large molecular assembly is held together: the original aggregate's size alone does not identify its binding partners.[ref]
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