Description

• General description: Clostridium histolyticum collagenases (CCH) are classified into two types ; I and II. Both are a single polypeptide with molecular weight of 114kDa - 113kDa, respectively. CCH I contains tandem domains and CCH II contain single domain for collagen binding.[1]
• Application: Collagenase from Clostridium histolyticum has been used in a study to investigate the degradation of collagen by the cariogenic bacteria, Streptococcus mutans. Collagenase from Clostridium histolyticum has also been used in a study to investigate the survivability of collagen micronetworks in the presence of collagenase.
• Biochem/physiol Actions: Clostridium histolyticum collagenase (CCH) is a digestive enzyme acting particularly on collagen. It is useful in the treatment of Dupuytren′s contracture, fibroproliferative disorder.[1]
• 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.
• Analysis Note: Also contains clostripain, nonspecific neutral protease, and tryptic activities.