Enhanced proteolysis of bovine fibrinogen in the presence of polysulfates.
Proteolysis of fibrinogen by bovine trypsin and chymotrypsin was enhanced by heparin, dextran sulfate (DS) and polyvinyl sulfate (PVS) in the presence of 0.1 M NaCl. Decrease in intrinsic fluorescence of fibrinogen with time was also enhanced by DS and PVS in the absence of NaCl, but not in the presence of 0.1 M NaCl. Thus, increase in susceptibility of fibrinogen to proteases in the presence of three polysulfate was more sensitive than time-dependent conformational change of the substrate protein.
D000818:Animals; D002417:Cattle; D002918:Chymotrypsin / Q000037:antagonists & inhibitors / Q000378:metabolism; D016264:Dextran Sulfate; D003911:Dextrans / Q000494:pharmacology*; D005340:Fibrinogen / Q000378:metabolism*; D005453:Fluorescence; D006493:Heparin / Q000494:pharmacology*; D006868:Hydrolysis; D007700:Kinetics; D010447:Peptide Hydrolases / Q000378:metabolism*; D011145:Polyvinyls / Q000494:pharmacology*; D012965:Sodium Chloride / Q000494:pharmacology; D014357:Trypsin / Q000378:metabolism
D003911:Dextrans; D011145:Polyvinyls; C019050:polyvinyl sulfate; D012965:Sodium Chloride; D005340:Fibrinogen; D006493:Heparin; D016264:Dextran Sulfate; D010447:Peptide Hydrolases; D002918:Chymotrypsin; D014357:Trypsin