X-ray fibre diffraction of cartilage proteoglycan aggregates containing hyaluronic acid (Short Communication) |
| |
| Authors: | E. D. T. Atkins T. E. Hardingham D. H. Isaac H. Muir |
| |
| Affiliation: | H. H. Wills Physics Laboratory, University of Bristol, Royal Fort, Tyndall Avenue, Bristol BS8 1TL, U.K.;Kennedy Institute of Rheumatology, Bute Gardens, Hammersmith, London W6 7DW, U.K. |
| |
| Abstract: | Ordered conformations of proteoglycan-hyaluronic acid aggregates in the intercellular matrix in cartilage were observed by X-ray diffraction. The sodium salt form of three samples, (a) aggregated proteoglycan, (b) disaggregated proteoglycan and (c) reconstituted disaggregated proteoglycan, give essentially similar X-ray fibre-type diffraction photographs. The patterns correlate with the chondroitin 4-sulphate component and can be interpreted as twofold helical conformations, similar to that observed previously for the free acid form of chondroitin 4-sulphate (Isaac & Atkins, 1973). The information takes us one step nearer the situation found in cartilage in vivo. |
| |
| Keywords: | |
|
|
