NON-COLLAGENOUS PROTEINS OF A RAT DENTIN MATRIX POSSESSING BONE MORPHOGENETIC ACTIVITY
NON-COLLAGENOUS PROTEINS OF A RAT DENTIN MATRIX POSSESSING BONE MORPHOGENETIC ACTIVITY
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DOI：
10.1177/00220345770560030601
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发表时间：
1977-01-01
影响因子：
7.6
通讯作者：
UYENO, S
中科院分区：
文献类型：
--
作者：
BUTLER, WT;MIKULSKI, A;UYENO, S
大鼠牙本质基质的不溶性制剂具有骨形态发生蛋白（BMP）活性，即，肌肉内植入时诱导软骨和骨形成的能力。由于BMP活性以前归因于骨和牙本质的非胶原蛋白（NCP），因此检查了大鼠牙本质的NCP的性质。用纯化的细菌胶原酶处理基质后，3种NCP溶解，同时牙本质胶原消化成较小的肽。3种蛋白质经离子交换层析分离。NCP 2富含天冬氨酸、谷氨酸、甘氨酸、丝氨酸和丙氨酸，因此显示出与其他结缔组织的酸性蛋白相似的组成。第三个NCP的氨基酸组成是天冬氨酸，丝氨酸丰富的磷蛋白，主要是在大鼠牙本质中的可溶性形式。这一观察结果支持了牙本质磷蛋白的一部分被牢固结合的观点。
An insoluble preparation of rat dentin matrix possessed bone morphogenetic protein (BMP) activity, i.e., the capacity to induce the formation of cartilage and bone when implanted intramuscularly. Since BMP activity was previously attributed to noncollagenous proteins (NCP) of bone and dentin, the nature of NCP of the rat dentin was examined. After treatment of the matrix with purified bacterial collagenase, 3 NCP were solubilized concomitantly with digestion of the dentin collagen to smaller peptides. The 3 proteins were separated by anion-exchange chromatography on DEAE-cellulose. Of the NCP 2 were rich in aspartate, glutamate, glycine, serine, and alanine, and thus displayed compositions similar to acidic proteins of other connective tissues. The 3rd NCP was shown by amino acid composition to be the aspartate, serine-rich phosphoprotein, which occurs mostly in a soluble form in rat dentin. This observation supports the view that a portion of dentin phosphoprotein is firmly bound.