Kleter G A, Damen J J, Kettenes-van den Bosch J J, Bank R A, te Koppele J M, Veraart J R, ten Cate J M
Department of Cariology Endodontology Pedodontology, Academic Centre for Dentistry Amsterdam (ACTA), Louwesweg 1, NL-1066 EA Amsterdam, Netherlands.
Biochim Biophys Acta. 1998 Jul 23;1381(2):179-90. doi: 10.1016/s0304-4165(98)00027-0.
The aim was to identify suspect collagen cross-links in dentine, eluting close to known cross-links in ion-exchange HPLC. Bovine tooth roots as source of dentine were powdered, demineralised, reduced, and acid-hydrolysed. Cross-linking amino acids were isolated from the acid hydrolysate by size exclusion, adsorption, and sequential ion exchange chromatography. In addition to dihydroxylysinonorleucine and hydroxylysylpyridinoline, an unknown cross-link was isolated (V-2). The ultraviolet, mass, and nuclear magnetic resonance spectra support the proposed structure of V-2, a trimeric amino acid with a pyrroleninone nucleus.
目的是在牙本质中鉴定可疑的胶原蛋白交联物，其在离子交换高效液相色谱中洗脱位置接近已知交联物。将牛齿根作为牙本质来源进行研磨、脱矿质、还原和酸水解。通过尺寸排阻、吸附和连续离子交换色谱法从酸水解产物中分离出交联氨基酸。除了二羟基赖氨酰正亮氨酸和羟赖氨酰吡啶啉外，还分离出一种未知的交联物（V-2）。紫外光谱、质谱和核磁共振光谱支持了V-2的 proposed 结构，即一种具有吡咯宁酮核的三聚体氨基酸。 （注：此处“proposed”原文未翻译完整，可能影响理解，完整翻译应为“提出的”）
