Nongelling components of gelatin should be mobile in the gel matrix if they were in sol form. To examine this an electric field was applied to a gelatin gel under the conditions where the gelatin carried sufficient net charge. Polypeptide fractions were obtained in the anodic buffer only if the electricity was introduced. This method might exclude effects of gel solubility on the composition of the extract. SDS electrophoretic analysis showed that the molecular-weight distribution of these extracts was mainly in the range of 10-70 k da. The amino acid composition of 5°C extract was compared to those of Type I collagen and its α2 chain. It could not be concluded to which reference the extract was more similar. We suppose that the electrophoretic extracts are not the same as cold water ones.