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

Conference ·
OSTI ID:5446726

Small-angle neutron scattering, SANS, of the proteoglycan subunit of bovine nasal cartilage in 0.15N LiCl at 25/sup 0/C yielded the radius of gyration, R/sub g/, radius of gyration of the cross-section, R/sub q/, persistence length, a, and the molecular weight, M. The following values were obtained: M = 3.9 x 10/sup 6/, R/sub g/ = 745 A, R/sub q/ = 34.6 A and a = 35.2 A. 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 D/sub 2/O showed a characteristic broad peak in the specified angular range similar to that observed from SAXS, thus confirming the polyelectrolyte nature of the proteoglycan. 15 refs., 3 figs., 1 tab. (DT)

Research Organization:
Stevens Inst. of Tech., Hoboken, NJ (USA). Dept. of Chemistry and Chemical Engineering; Rockefeller Univ., New York (USA); Oak Ridge National Lab., TN (USA)
DOE Contract Number:
AC05-84OR21400
OSTI ID:
5446726
Report Number(s):
CONF-850871-7; ON: DE85016935
Resource Relation:
Conference: International conference on neutron scattering, Santa Fe, NM, USA, 19 Aug 1985; Other Information: Portions of this document are illegible in microfiche products
Country of Publication:
United States
Language:
English