Description

• Application: Collagenase from Clostridium histolyticum has been used: to harvest osteosarcoma 143B cells from collagen scaffold[1]in tissue digestion of islets[2] and carotid artery[3]in the digestion of chorionic villi[4]in enzymatic dissociation for ATP-based tumour chemosensitivity assay (ATP-TCA) in solid tumors[5]
• Biochem/physiol Actions: Clostridium histolyticum produces two classes of collagenases. Clostridial collagenases are found to be highly effective than mammalian collagenases. It is capable of cleaving at multiple cleavage sites within the collagen triple helix. It is implicated in the bacterial invasion in gas gangrene.[6]
• Unit Definition: One collagen digestion unit (CDU) liberates peptides from collagen from bovine achilles tendon equivalent in ninhydrin color to 1.0 μmole of leucine in 5 hours at pH 7.4 at 37 °C in the presence of calcium ions. One FALGPA hydrolysis unit hydrolyzes 1.0 μmole of furylacryloyl-Leu-Gly-Pro-Ala per min at 25°C. One Neutral Protease unit hydrolyzes casein to produce color equivalent to 1.0 μmole of tyrosine per 5 hr at pH 7.5 at 37°C. One Clostripain Unit hydrolyzes 1.0 μmole of BAEE per min at pH 7.6 at 25°C in the presence of DTT.