3.4.17.2	Fibrin + H2O	CPB activity generates fine-mesh fibrin which is more difficult to lyse by tPA	
3.4.17.2	human proinsulin + H2O	enzymatic modification of human proinsulin using trypsin and carboxypeptidase B generally causes high accumulation of insulin derivatives, leading to more complicated purification processes. A simple method including citraconylation and decitraconylation in the enzymatic modification process is developed for the reduction of a major derivative, des-threonine human insulin	
3.4.17.2	additional information	the enzyme plays a role in the fibrinolytic or coagulation system	
3.4.17.2	additional information	mechanism for the antifibrinolytic affect of the plasma enzyme	
3.4.17.2	additional information	active carboxypeptidase B is present in free form in serum from patients with acute pancreatitis	
3.4.17.2	additional information	the enzyme is highly specific for excising C-terminal Lys and Arg residues from peptides and proteins with a preference for Arg, it also acts on C-terminal Val, Leu, Ile, Asn, Gly, and Gln but at a slower rate, the enzyme shows a preference for Ala in P2 position	
3.4.17.2	additional information	the enzyme is involved in digestion processes in the gut supplying free amino acid for developing larvae	
3.4.17.2	OPN-R + H2O	osteopontin (OPN) gets activated by thrombin resulting in OPN-R. OPN-R is subsequently inactivated by CPB generating OPN-L