Comparative studies of phosphoprotein preparations from rat incisor dentin.

Comparative studies of phosphoprotein preparations from rat incisor dentin.
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大鼠切牙牙本质磷蛋白制剂的比较研究。

DOI:
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发表时间:
1980
期刊:
Preparative Biochemistry
影响因子:
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通讯作者:
L. Lundvik
L. Lundvik
中科院分区:
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文献类型:
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作者:
M. Jontell;A. Linde;L. Lundvik

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采用醋酸脱矿后提高离子强度提取和中性EDTA溶液脱矿同时提取两种方法从大鼠门牙本质中提取磷蛋白。通过Sepharose 4B和deae -纤维素层析纯化溶解蛋白。聚丙烯酰胺凝胶电泳的材料从两种制剂产生一个单带。除了氨基酸分析外,没有证据表明两种磷蛋白制剂之间存在差异。通过等电聚焦进一步纯化后,氨基酸分析显示了相似的组成。结果表明,两种方法提取的磷蛋白在适当的纯化条件下可得到相同的产物。该研究没有给出任何明确的答案,是否有任何磷蛋白成分存在于大鼠门牙本质是共价连接到胶原基质。
Phosphoprotein was obtained from rat incisor dentin either by extraction at elevated ionic strength after acetic acid demineralization, or by extraction simultaneous with demineralization in neutral EDTA solution. Purification of solubilized proteins was achieved by Sepharose 4B and DEAE-cellulose chromatography. Polyacrylamide gel electrophoresis of the material from the two preparations resulted in one single band. Except for the amino acid analyses, no evidence for a difference between the two phosphoprotein preparations could be found. After additional purification by iso-electric focusing the amino acid analyses demonstrated a similar composition. It is concluded that the two methods for phosphoprotein extraction yield the same product when purified properly. The study did not give any unequivocal answer as to if any phosphoprotein component exists in rat incisor dentin which is covalently linked to the collagen matrix.