Comparasion of hydrolytic activity of cardosin A and B on Collagen i

Recently it was described the isolation and characterization of two new aspartic proteases isolated from the flowers of cardoon (Cynara cardunculus L.), cardosin A and cardosin B. These enzymes exhibit a high specificity for bonds between hydrophobic aminoacids. Both enzymes can perform a restrict hydrolysis of interstitial collagen molecules at a cellular pH. This hydrolytic activity can be useful for the treatment of some pathologic conditions, such as fibrosis. Cardosin A and cardosin B were used to perform in vitro hydrolysis of non denaturated collagens I (from Sigma) . The reactions were performed in citrate-phosphate buffer 100 mM at pH 5.5, at 37oC, for 24 hours. The results of the hydrolysis reaction were followed by SDS-PAGE in Mini-protean II (BioRad). We observed restrict in vitro hydrolisis of the collagen molecules with both enzymes. These two enzymes, alghouh with very closed specificities, they produce different peptide fragments. These enzymes have a true potential for further studies in order to be included in the strategies of treatment of fibrosis.