Cohen-Solal L, Glimcher M
C R Acad Hebd Seances Acad Sci D. 1977 Jun 6;284(21):2155-8.
Phosphoproteins of Chicken bone have been extracted by 0.5 M EDTA pH 7.5. Their amino acid composition was similar to that of phosphoproteins of other calcified tissues. The crude EDTA extract contained 80 to 90% proteins, only 70% of the total organic phosphorus was bound to the proteins. We have studied and identified two phosphorylated components. o-phosphoserine and o-phosphothreonine have been identified by amino acid analysis at pH 1.7 from a partial acid hydrolysate, and confirmed by the liberation of the parent amino acids after total hydrolysis. In addition, phosphorus was found equimolecular to both of them. The presence of these phosphorylated groups is important for an understanding of the role of these proteins in the mechanism of mineralization.
鸡骨磷蛋白已用0.5M pH 7.5的乙二胺四乙酸（EDTA）提取。它们的氨基酸组成与其他钙化组织的磷蛋白相似。粗EDTA提取物含有80%至90%的蛋白质，仅70%的总有机磷与蛋白质结合。我们研究并鉴定了两种磷酸化成分。通过对部分酸水解产物在pH 1.7下进行氨基酸分析鉴定出了O-磷酸丝氨酸和O-磷酸苏氨酸，并在完全水解后通过母体氨基酸的释放得到了证实。此外，发现磷与它们两者的分子数相等。这些磷酸化基团的存在对于理解这些蛋白质在矿化机制中的作用很重要。
