Abstract
A method is described for the cleavage of collagenous molecules by bacterial collagcnase in the presence of sodium dodecyl sulphate (SDS) and urea. Comparison of three commercially available preparations of bacterial collagenase showed that the most efficient cleavage under these conditions was by the enzyme isolated from Achromobacter iophagus (E.C. 3.4.24.8). No non-specific proteinase activity was apparent in conditions where all collagen types showed some susceptibility to attack. This method represents a simple one-stage identification of collagenous molecules in complex mixtures of proteins and where limited amounts of a protein are available.