A Species Comparative Study of the Soluble Phosphoproteins of Dentin.

The soluble phosphoproteins of the dentin have been isolated from the rabbit, cow, hog, and human. The phosphoproteins were purified by means of gel filtration and anion-exchange chromatography, and polyacrylamide gel electrophoresis. They all showed high levels of aspartic acid, serine, and phosphate which is bound as phosphoserine. The data do not clearly suggest that a dentin phosphoprotein exists in the fish. The phosphoprotein of dentin may be a high molecular weight aggregate of greater than 150,000 daltons.The phosphoproteins purified in this study compare reasonably to the majority of the soluble and insoluble phosphoproteins isolated by other investigators.The findings of this study suggest that similar phosphoproteins are found in almost all mineralizing dentin. When combined with other electron and light microscopic and radioautographic data, the data of this study suggest that the dentin phosphoproteins are involved in the mineralization process. Radioautography in conjunction with electron microscopy would help to further support this hypothesis.

Level thesis:degree_level

Thesis

Year

1976

Author dc:creator

• Beegle, William Frederick

• Phosphoproteins
• Dentin

Repository record dc:identifier

https://digitalcommons.library.uab.edu/etd-collection/7003

OAI identifier oai:identifier

oai:digitalcommons.library.uab.edu:etd-collection-7995