Thermal Contraction of Collagen and its Dissolution with Elastase

THE observation of Dr. Banga that thermally contracted tendon collagen is dissolved under the action of elastase is obviously of great importance. There is considerable evidence that elastin preparations from aorta and from ox ligament, even after the presumed removal of collagen, do not present single substrates to the action of elastase 1 . In the course of a search for a purer substrate for elastase, we have also observed the dissolution of thermally contracted collagen both from Achilles tendon and from rat tail tendon. In addition we have found that elastase, acting at p H 8.7, causes the dissolution of the water-insoluble protein in bovine crystalline lens and of the lens capsule. The dissolution of lens capsule is particularly interesting, since the material shows some similarity in amino-acid composition to collagen, its X-ray diffraction pattern is like that of a partially oriented collagen, it contains much polysaccharide and has a definite marked shrinkage temperature between 60° and 70° 2 . We have thus shown that elastase will attack a collagenous material even when it has not been thermally contracted.