Human Epidermal Transglutaminase: Preparation and Properties

The study focused on purifying a transglutaminase enzyme from human hair follicle-free epidermis and analyzing its properties. The enzyme had varying molecular weights depending on the method used, and it was capable of cross-linking fibrinogen in the absence of Factor XIII. Calcium or strontium was essential for its activity, which could be enhanced by heat or dimethylsulfoxide. Activation of the enzyme required calcium and was not inhibited by serine protease inhibitors. Both the native and activated forms of the enzyme showed similar substrate affinity, but the activated form had a larger elution volume in gel filtration. The exact mechanism of activation was not determined.