Serological Evidence for a Specific Clostridium histolyticum Gelatinase

SUMMARY: Evidence is presented that a specific gelatinolytic enzyme besides collagenase is present in purified Clostridium histolyticum collagenase preparations. This means that collagenase itself need not be able to digest gelatin but it does not exclude the possibility. The purest collagenase available to date (DeBellis, Mandl, MacLennan & Howes, 1954) is free of non-specific proteolytic activity and active only against collagen and collagen degradation products (azocoll, gelatin). The question whether these activities are due to the same enzyme, i.e. whether collagenase will break down gelatin as well as collagen is still unsolved. It is possible that a series of reactions catalysed by distinct enzymes is involved but that our ana-lytical procedures are inadequate for the detection of the primary effect of collagenase. This may involve simple breaking of hydrogen bonds as in urea treatment which results in denatured collagen susceptible to enzymes such as trypsin. However, the entire collagenase system differs from such proteinases by its specificity and complete lack of reaction with other proteins such a