Multinuclear nuclear magnetic resonance spectroscopic study of cartilage proteoglycans
Hyaline cartilage is a composite material whose major function is to withstand compression while retaining flexibility. Its mechanical properties are affected by tissue hydration and ionic composition. Models of the mechanical behavior of cartilage have incorporated certain assumptions about the interactions of the major components of cartilage: collagen, proteoglycans, water, and cations. To determine the validity of these assumption, the authors have used nuclear magnetic resonance spectroscopy (NMR). Two approaches have been used: (a) natural abundance carbon-13 NMR; and (b) NMR of sodium-23, potassium-39, magnesium-25, and calcium-43. Evidence from studies in intact tissues are reinforced by extensive measurements on solutions of proteoglycans and other relevant macromolecules. Based on the measurements of NMR relaxation rates and lineshapes reported here, it is concluded that neither sodium nor potassium interact strongly with bovine nasal proteoglycan aggregates or their substituent glycosaminoglycan chains in solution. Proteoglycans do bind magnesium and calcium. Therefore there is a qualitative difference between monovalent and divalent cations, which is not taken into account by polyelectrolyte models or models for the ionic dependence of mechanical properties. Cation binding to heparin, which has a higher charge density than cartilage proteoglycans, was also studied. The results presented here establish that heparin binds sodium, magnesium, and calcium.
- Research Organization:
- Johns Hopkins Univ., Baltimore, MD (USA)
- OSTI ID:
- 6985730
- Resource Relation:
- Other Information: Thesis (Ph. D.)
- Country of Publication:
- United States
- Language:
- English
Similar Records
Patterns of proteoglycan degradation by a neutral protease from human growth-plate epiphyseal cartilage
Visualization of sulfur-containing components associated with proliferating chondrocytes from rat epiphyseal growth plate cartilage: Possible proteoglycan and collagen co-migration
Related Subjects
GLUCOPROTEINS
NUCLEAR MAGNETIC RESONANCE
CALCIUM 43
CARBON 13
CARTILAGE
CATTLE
HEPARIN
MAGNESIUM 25
NMR SPECTRA
POTASSIUM 39
SODIUM 23
ALKALI METAL ISOTOPES
ALKALINE EARTH ISOTOPES
AMINES
ANIMAL TISSUES
ANIMALS
ANTICOAGULANTS
BODY
CALCIUM ISOTOPES
CARBOHYDRATES
CARBON ISOTOPES
CONNECTIVE TISSUE
DOMESTIC ANIMALS
DRUGS
EVEN-ODD NUCLEI
HEMATOLOGIC AGENTS
INTERMEDIATE MASS NUCLEI
ISOTOPES
LIGHT NUCLEI
MAGNESIUM ISOTOPES
MAGNETIC RESONANCE
MAMMALS
MUCOPOLYSACCHARIDES
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
POLYSACCHARIDES
POTASSIUM ISOTOPES
PROTEINS
RESONANCE
RUMINANTS
SACCHARIDES
SODIUM ISOTOPES
SPECTRA
STABLE ISOTOPES
TISSUES
VERTEBRATES
550201* - Biochemistry- Tracer Techniques