Bovine ameloblast cell layer was incubated in 3H-proline containing medium and the incorporation of radioactivity into protein fractions of the cell and the medium was investigated by SDSpolyacrylamide gel electrophoresis.
The results suggest that the ameloblasts synthesize and secrete a protein having a molecular weight of 25,000 daltons which is supposed to be the prototype of enamel proteins. This protein was degraded into dialyzable sizes by the cell extract. After a longer period of incubation another low molecular weight protein fraction appeared in the medium.
Purification procedure with SDS gel filtration of the enamel protein is reported.
Get full access to this article
View all access options for this article.
References
1.
Weber, K., Osborn, M.: J Biol Chem244:4406-4412, 1969.
