Studies were carried out on the use of disc electrophoresis on polyacrylamide gel to analyze protein binders. Standard electrophoregrams were made of seven binders -- hide glue, gelatine, sturgeon glue, egg white, egg yolk, oat paste, and rye flour paste. The proteins were then sub-jected to aging by means of UV radiation, oxygen and temperature control. The results have shown the usefulness of this method as a way of identifying protein binders. One problem in identification, however, was differentiating hide glue from gelatine; this was due to the presence of collagen. Advantages of this method are accuracy and the need for such small samples. It is suggested that this technique will be acceptable to both conservators and analytical chemists.