Abstract
Addition of aprotinin in human and rat pancreatic extracts inactivates nonspecific proteases that completely degrade collagen. We sought to clarify the relative roles of collagenase and nonspecific proteases in the breakdown of collagen by the pancreas. The degradation of [3H] collagen fibrils by pancreatic extracts to small fragments of low molecular weight was determined by SDS-electrophoresis and autoradiography. Aprotinin (0.14 mg/mL) was added to inhibit nonspecific protease activity. Rat and human pancreas extracts contained a high collagenolytic activity that was demonstrated to be the result of the combined action of collagenase and other pancreatic proteases. Seventy percent of the total collagenolytic activity in rat pancreas extracts was inhibited by aprotinin. The same aprotinin concentration had no effect on two commercially available collagenases. The electrophoretic pattern obtained from [3H] collagen treated with rat and human pancreatic extracts containing aprotinin confirmed the presence of a true specific collagenase in the pancreas.
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