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]
Aggregation of Cartilage Proteoglycans: III. Characteristics of the Proteins Isolated from Trypsin Digests of Aggregates by D. Heinegård and others. Journal of Biological Chemistry 249, pp. 4250–4256; summary and experimental fractionation
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]
Aggregation of Cartilage Proteoglycans: III. Characteristics of the Proteins Isolated from Trypsin Digests of Aggregates by D. Heinegård and others. Summary; hyaluronic-acid binding of separated fractions
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