The authors of the present work have carried out studies on the use of disc electrophoresis on polyacrylamid gel to analyze protein binders. Standard electrophoregrams were made of seven binders (hide glue, gelatine, sturgeon glue, egg white, egg yolk, glue from oats and from rye flour). The proteins were then subjected to aging by means of UV radiation, oxygen and temperature. The results obtained have shown the usefulness of the examined method as a way of identifying protein binders. The only identification problem was to differentiate hide glue from gelatine, although this difficulty was due to the fact that an initial protein was collagen from mammals. In the majority of cases, disc electrophoresis on polyacrylamid gel has been found very useful. One of the biggest advantages of that method is the confidence in identification and small quantities of samples necessary to make the analysis (from 20 to 50 mg of protein). It may be believed that this method shall become a compromise between the interests of conservators and of analytical chemists.
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