The Preparation of Soft-Tritium-Labeled Proteins and Their Application for the Collagenolytic Activity Investigations

Abstract Tritium-labelled Type I collagen from rat skin with specific activity of 8 mCi/mg and mixture of the crab hepatopancrease collagenolytic enzymes with specific activity of 25 mCi/mg have been obtained by the method of high-temperature solid-state catalytic isotope exchange (HSCIE) without loss of native features. Tritium-labelled Type I collagen kept its ability to form native fibrills being resistant to trypsin hydrolysis. Tritium-labelled collagenase keeps about 70% of its proteolytic activity.