Kuboki Y, Fujisawa R, Tsuzaki M, Liu C F, Sasaki S
Calcif Tissue Int. 1984 Jan;36(1):126-8. doi: 10.1007/BF02405305.
Trypsin digestion and successive calcium-induced precipitation of the insoluble bovine dentin matrix effectively separated the collagen and phosphoprotein fractions which were firmly associated together in this material. Amino acid analysis by four different systems revealed that the lysinoalanine and histidinoalanine, which had been previously reported to occur in the human dentin collagen, were concentrated in the phosphoprotein fraction but were not present in the collagen fraction. Furthermore, it was found that the free-type phosphoprotein which was isolated from EDTA extract of dentin powder also contained both "cross-linking" amino acids. The results indicated the both "cross-links" distributed within the dentin phosphoprotein and were not likely to contribute the unique stability of dentin collagen.
胰蛋白酶消化以及随后对不溶性牛牙本质基质进行钙诱导沉淀，有效地分离了胶原蛋白和磷蛋白部分，这两种成分在该材料中紧密结合在一起。通过四种不同系统进行的氨基酸分析表明，先前报道在人牙本质胶原蛋白中出现的赖氨酰丙氨酸和组氨酰丙氨酸集中在磷蛋白部分，而在胶原蛋白部分中不存在。此外，还发现从牙本质粉末的EDTA提取物中分离出的游离型磷蛋白也含有这两种“交联”氨基酸。结果表明，这两种“交联”分布在牙本质磷蛋白中，不太可能有助于牙本质胶原蛋白的独特稳定性。
