Gelatin is the degradation product of the protein collagen. During commercial production, the noncovalent interactions and covalent cross-links which stabilise the molecular structure of collagen are cleaved, yielding a preparation containing components with a wide range of molecular weights. Aqueous B225, B60 and A60 gelatin solutions (0.2% w/v) were analysed by size exclusion HPLC and the chromatograms were evaluated both by the Peakfit™ Gaussian deconvolution software program and by traditional perpendicular dropping, the different components being grouped into previously determined molecular weight classes. The data obtained were validated using a static light scattering technique. The results show that while deconvolution gives results that are statistically identical to those obtained by perpendicular dropping, it does not offer a significant advantage as a means of analysing complex gelatin chromatograms.