Small-angle neutron scattering studies from solutions of bovine nasal cartilage proteoglycan

Abstract

Small-angle neutron scattering, SANS, of the proteoglycan subunit of bovine nasal cartilage in 0.15 N LiC1 at 25°C yielded the radius of gyration, Rg, radius of gyration of the cross-section, Rq, persistence length, a*, and the molecular weight, M. The following values were obtained: M = 3.9 × 106, Rg = 745 Å, Rq = 34.6 Å and a* = 35.2 Å. These values compare favorably with those that were obtained from small angle X-ray scattering, SAXS, of a similar extract. The scattering curve of the proteoglycan subunit in D2O showed a characteristic broad peak in the specified angular range similar to that observed from SAXS, thus confirming the polyelectrolyte nature of the proteoglycan.