High-resolution solid-state nuclear magnetic resonance spectra of dentin collagen.
Insoluble collagen of bovine dentin was characterized by high-resolution solid-state 13C nuclear magnetic resonance (NMR) spectroscopy using a cross-polarization magic angle spinning procedure. A downfield shift was observed in the signal of hydroxyproline C beta compared with that in skin collagen, indicating a distortion in the hydroxyproline structure. A signal of 31P NMR was detected in dentin collagen that was compatible with the presence of matrix-associated phosphoprotein.
Fujisawa
R
R
Dept. of Biochemistry, School of Dentistry, Hokkaido University, Sapporo, Japan.
Kuboki
Y
Y
D000818:Animals; D001842:Bone and Bones; D002247:Carbon Isotopes; D002417:Cattle; D003094:Collagen / Q000302:isolation & purification; D003804:Dentin; D007180:Incisor; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D009928:Organ Specificity; D011487:Protein Conformation; D012867:Skin; D013710:Tendons; D013977:Tibia
D002247:Carbon Isotopes; D003094:Collagen