Effects of different extraction media on the electrophoretic pattern of proteins from partly mineralized bovine enamel.

Five different extraction solutions were used to isolate matrix proteins from immature bovine enamel, to evaluate the effect of this procedure on the pattern obtained after electrophoresis. By sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the dominating protein fraction in the ethylenediaminetetraacetic acid extract had a molecular weight of 67,000 daltons. The acetic acid and phosphate buffer extracts contained mostly low molecular weight proteins. Isoelectric focusing showed that most of the enamel proteins had isoelectric points below pH 7.0.