SUBSTRATE-SPECIFICITY OF COLLAGENOLYTIC PROTEASES FROM THE KING CRAB PARALITHODES CAMTSCHATICA

Substrate specificity of two collagenolytic proteases from the king cr ab Pavalithodes camtschatica has been studied. Both proteases are show n to hydrolyze effectively type I and III collagens, gelatin and fibri nogen. The variety of products formed during the enzymatic hydrolysis of the proteins appeared to be different for crab proteases A and C. S tudies on peptide hydrolysis demonstrated that protease A cleaves pref erably peptide bonds with Arg and Lys as carbonyl components, while pr otease C prefers hydrophobic amino acids. Kinetic constants of hydroly sis for low molecular weight substrates in the presence of crab protea ses have been determined. This allowed us to characterize collagenolyt ic protease A as a trypsin-like protease. By contrast, collagenolytic protease C was classified as chymotrypsin-like protease although this protease and bovine chymotrypsin are not completely similar. Collagena se substrates Pz-Pro-Leu-Gly-Pro-D-Arg and Z-Gly-Pro-Ala-Gly-Pro-Ala w ere found to be resistant to both crab proteases.