The rotary-shadowing technique for molecular electron microscopy was used to study cartilage proteoglycan structure. The high resolution of the method allowed demonstration of two distinct globular domains as well as a more strand-like portion in the core protein of large aggregating proteoglycans. Studies of proteoglycan aggregates and fragments showed that the globular domains represent the part of the proteoglycans that binds to the hyaluronic acid, i.e. the hyaluronic acid-binding region juxtapositioned to the keratan sulphate-attachment region. The strand-like portion represents the chondroitin sulphate-attachment region. Low-Mr proteoglycans from cartilage could be seen as a globule connected to one or two side-chain filaments of chondroitin sulphate.
Domain structure of cartilage proteoglycans revealed by rotary shadowing of intact and fragmented molecules
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H Wiedemann, M Paulsson, R Timpl, J Engel, D Heinegård; Domain structure of cartilage proteoglycans revealed by rotary shadowing of intact and fragmented molecules. Biochem J 15 November 1984; 224 (1): 331–333. doi: https://doi.org/10.1042/bj2240331
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