Dodd C M, Carmichael D J
Biochim Biophys Acta. 1979 Mar 27;577(1):117-24. doi: 10.1016/0005-2795(79)90013-8.
Predentine obtained from bovine teeth by microdissection was solubilized by cyanogen bromide cleavage. The electrophoretic mobility of the resultant peptides was established on polyacrylamide gel and the amino acid composition of several peptides was determined. The data clearly indicated that this collagen is entirely of the Type I genetic species. No differences were detected between the predentine and dentine collagens except that the mature tissue was more highly crosslinked. Nevertheless the amount of stable cross-link formed in the predentine was higher than expected for an immature tissue.
通过显微切割从牛牙中获得的前期牙本质经溴化氰裂解使其溶解。在聚丙烯酰胺凝胶上确定所得肽段的电泳迁移率,并测定了几种肽段的氨基酸组成。数据清楚地表明,这种胶原蛋白完全属于I型基因种类。除了成熟组织交联程度更高外,前期牙本质和牙本质胶原蛋白之间未检测到差异。然而,前期牙本质中形成的稳定交联量高于未成熟组织的预期值。