Abstract
Conclusions and summary
From these data, it is apparent that whole activated pancreas, unlike pancreatic juice, contains a thermo-labile material which can reduce by 50% both viscosity and ability to form fibers of acid soluble collagen solutions. This activity is not affected by various trypsin inhibitors, nor is it duplicated by trypsin, elastase, chymotrypsin or hyaluronidase alone. This activity may be due to a new enzyme in the pancreas, a collagenase. In view of lack of activity of this enzyme upon serum and egg albumin, casein and gelatin, this enzyme would seem to be reasonably specific for acid soluble collagen.
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