The proteolytic action of bacterial proteases from Clostridium histolyticum on bovine fibrinogen.
Bacterial proteases from Clostridium histolyticum bring about the polymerization of fibrinogen into structured fibres, the period being 9 nm when the ionic strength (I)  of the solution is between 0.1 and 0.2. At I=0.3 no polymerization occurs, but the successive actions of bacterial proteases and thrombin induce polymerization, the fibres obtained showing a periodic structure: the major period is 23 nm with two minor striations. The striation pattern is different from that obtained with fibrin which shows a major period of 23 nm with three minor striations. The degree of degradation of fibrinogen monitored by disc gel electrophoresis shows that the Aalpha polypeptide chain (mol. wt.=68 000) is degraded into Aalpha1 (mol. wt.=32 000) and Aalpha2 (mol. wt.=29 000), whilst the mobility of Bbeta increases and gamma remains unchanged; the molecular weight is estimated between 272 000 and 269 000. These results emphasize that the charge distribution differences which are compatible with the loss of different portions of the molecule, lead to variations in fibre structures.
D000818:Animals; D002364:Caseins / Q000032:analysis; D002417:Cattle; D003013:Clostridium / Q000201:enzymology*; D003545:Cysteine / Q000494:pharmacology; D005340:Fibrinogen / Q000378:metabolism*; D003012:Microbial Collagenase / Q000032:analysis; D008854:Microscopy, Electron; D010447:Peptide Hydrolases / Q000378:metabolism*; D011108:Polymers; D013329:Structure-Activity Relationship
D002364:Caseins; D011108:Polymers; D005340:Fibrinogen; D010447:Peptide Hydrolases; D003012:Microbial Collagenase; D003545:Cysteine