Fujisawa R, Kuboki Y
Dept. of Biochemistry, School of Dentistry, Hokkaido University, Sapporo, Japan.
Biochem Biophys Res Commun. 1990 Mar 16;167(2):761-6. doi: 10.1016/0006-291x(90)92090-m.
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.
采用交叉极化魔角旋转技术，通过高分辨率固态¹³C核磁共振（NMR）光谱对牛牙本质的不溶性胶原蛋白进行了表征。与皮肤胶原蛋白相比，羟脯氨酸Cβ信号出现了向低场的位移，表明羟脯氨酸结构发生了畸变。在牙本质胶原蛋白中检测到了³¹P NMR信号，这与基质相关磷蛋白的存在相符。
