Fincham A G, Belcourt A B, Lyaruu D M, Termine J D
Calcif Tissue Int. 1982 Mar;34(2):182-9. doi: 10.1007/BF02411231.
The matrix proteins of the developing dental enamel of five mammalian species were isolated and subjected to chromatographic, electrophoretic, and amino acid analyses. It was found that the principal chromatographic fractions showed similarities of both size and amino acid composition among species. The major amelogenin protein of the cow, hamster, human, and sheep was of about 30,000 daltons and of the pig enamel matrix about 20,000 daltons. In each species a higher molecular weight fraction, greater than 40,000 daltons, was detected. In the lower molecular weight range an amelogenin polypeptide enriched in leucine, a fraction rich in tyrosine, and a fraction of intermediate size (Bovine matrix "Component-14") were identified in each case. It is suggested that these characteristic proteins arise during the degradation of the matrix which accompanied mineralization.
分离出了五种哺乳动物发育中牙釉质的基质蛋白，并对其进行了色谱分析、电泳分析和氨基酸分析。结果发现，主要的色谱组分在物种间表现出大小和氨基酸组成的相似性。牛、仓鼠、人类和绵羊的主要釉原蛋白约为30,000道尔顿，猪牙釉质基质的主要釉原蛋白约为20,000道尔顿。在每个物种中都检测到了分子量大于40,000道尔顿的较高分子量组分。在较低分子量范围内，每种情况下都鉴定出了富含亮氨酸的釉原蛋白多肽、富含酪氨酸的组分以及中等大小的组分（牛基质“组分-14”）。有人认为，这些特征性蛋白质是在矿化过程中伴随基质降解而产生的。
