X-ray fibre diffraction of cartilage proteoglycan aggregates containing hyaluronic acid.
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.
D000818:Animals; D002807:Chondroitin / Q000032:analysis; D006025:Glycosaminoglycans / Q000032:analysis*; D006820:Hyaluronic Acid / Q000032:analysis*; D007633:Keratins / Q000032:analysis; D007830:Larynx / Q000032:analysis; D011509:Proteoglycans / Q000032:analysis*; D013552:Swine; D014961:X-Ray Diffraction
D006025:Glycosaminoglycans; D011509:Proteoglycans; D007633:Keratins; D006820:Hyaluronic Acid; D002807:Chondroitin