人胚牙釉质蛋白质的分离纯化

Separation and Purification of Human Fetal Enamel Proteins

选择5～9月龄人胚标本,按照 Lyaruu 方法分离出与牙釉质晶体结合疏松的釉原蛋白及结合紧密的釉蛋白。经葡聚糖凝胶 G—75层析后得到初步纯化的牙釉质蛋白质。釉原蛋白经凝胶柱层析后可分成9种组份,其分子量范围为5000～65500,主要的两种釉原蛋白分子量为22000及13000;釉蛋白可分成4种组份,分子量为10000～50000。从牙釉质蛋白质的氨基酸分析发现,釉原蛋白富合脯氨酸、谷脯酸及甘氨酸,而釉蛋白则含较多的丝氨酸、天门冬氨酸、甘氨酸及异亮氨酸。

Fresh human fetal dentitions were isolated from approximately 5 to 9 months fetus.Theauthors separated the amelogenins which loosely associated with mineral phase,and enamelinswhich closely associated with the mineral crystals by Lyaruu's method,these proteins werepartially purified with Sephadex G-75 gel filtration chromagraphy.The results show:Amel-ogenins are resolved into nine fractions eluted from the column,the molecular weights of thetwo main components are estimated as 22000 Da and 13000 Da.The elution curve of ename-lins has four peaks,the range of molecular weights are 10000 to 50000 Da.The authors alsoanalyse the amino acid composition of the enamel proteins,it shows that amelogenins areriched in procine,glutamic acid and glycine,enamelins are riched in serine,aspartic acid,glutamic acid,glycine and isoleucine.