Cleavage of bovine skin type III collagen by proteolytic enzymes. Relative resistance of the fibrillar form.

摘要: We have studied the susceptibility of fibrils formed from fetal bovine skin type III collagen to proteolytic enzymes known cleave within helical portion molecule (vertebrate and microbial collagenase, polymorphonuclear elastase, trypsin, thermolysin) two general proteases broad specificity (plasmin, Pronase). Fibrils reconstituted neutral salt solutions, at 35 degrees C, were highly resistant nonspecific proteolysis by such as thermolysin but rapidly dissolved bacterial vertebrate collagenases rates 12-45 mol X mol-1 h-1. In solution, was readily cleaved each (with exception plasmin), well true collagenases, although different rates. Turnover numbers determined viscometry C were: human approximately equal 1500 h-1; (clostridial) 100 proteases, 23-52 addition it shown that pronase cleaves in solution 22 attacking same Arg-Gly bond alpha 1(III) chain trypsin. However, like other Pronase rather ineffective against fibrillar forms collagen. It also transition I form resulted a significant gain triple thermostability evidenced 6.8 increase denaturation temperature (Tm = 40.2 solution; Tm 47.0 fibrils).