Protein glycation leads to the generation of advanced glycation end products (AGE). AGEs are implicated in the pathogenesis of chronic diabetic complications and age-related disorders. Some AGEs lead to protein cross-linking, affecting the protein function irreversibly. Long-lived predominantly found proteins such as collagen are primarily affected due to glycation-induced damage. Assessment of the antiglycation potential of substances requires costly equipment. A simple procedure is established to monitor glycation-induced protein cross-linking inhibitory potential of medicinal plants using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). SDS-PAGE separates proteins according to their molecular size. As the cross-linked products formed due to glycation-induced damage are stable under denaturing conditions and are of high molecular weight, such products can be separated and detected using SDS-PAGE. As the degree of high molecular weight products observed is proportionate to the extent of glycation-induced damage, SDS-PAGE can be used to monitor the potential of medicinal plants to inhibit glycation-induced protein cross-linking.