Enzymatic Proteolysis of Rat Sponge Biopsy Collagen Tissue

Abstract

Comments and summary

Pretreatment of rats with estrogen and relaxin does not appear to alter the susceptibility of sponge-biopsy connective tissue to digestion by proteolytic enzymes at near physiologic pH. No difference was noted in the proteolysis of collagen obtained from either sex or from castrate rats. Trypsin, Chymotrypsin and Papain all have a slight proteolytic activity on pretreated or untreated tissue, while pure Elastase and Hy-aluronidase effect little, if any, liberation of collagen. Impure Elastase dissolves 2 to 6 times the amount of collagen digested by the proteolytic enzymes or a combination of pure Elastase and Trypsin. It is postulated that the impure Elastase, prepared from pancreas, contains a collagenolytic enzyme distinct from the proteolytic enzymes of the pancreas. The removal of a portion of the scleroprotein of connective tissue by enzyme action results in a residue richer in hydroxyproline (per unit protein) than in the enzyme-free controls. This may occur either through the removal of a non-collagenous, saline-insoluble protein liberated by the enzyme, or through the selective removal of a type of collagen which has a lower hydroxyproline concentration than the tissue as a whole.