Abstract
Collagenolytic activity from normal human skin and human hypertrophic scar tissue are inhibited by protease inhibitors isolated by immobilized trypsin affinity chromatography from bovine cartilage and bovine aorta. The collagenase inhibitors are of low molecular weight (approximately 11,000) and are cationic proteins. Other trypsin inhibitors such as the bovine basic pancreatic trypsin inhibitor (Kunitz) as Trasylol R and soybean trypsin inhibitor show only minimal effects on collagenase activities. Human skin collagenase is inhibited by a protein (protease-inhibitor) obtained from human cartilage using human skin collagen as substrate. The inhibitors described may function in the physiological regulation of collagenase activity in connective tissues.
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