Electrophoretic separated matrix proteins from partly mineralized bovine enamel were stained by Coomassie blue and silver techniques. Conventional Coomassie staining was sufficient for demonstration of high molecular weight proteins on SDS PAGE. A Coomassie blue G-formaldehyde mixture was suitable for detection of the low-molecular-weight proteins. This staining mixture is also suitable for visualization of enamel proteins in isoelectric-focused gels. The high resolution of two dimensional electrophoresis is proved on the 67,000-dalton enamel protein fraction. Silver staining is superior to Coomassie blue for detection of small amounts of enamel proteins. A combination of Coomassie blue and silver staining result in very sharp bands on SDS PAGE.