3.4.21.7	Aprotinin	augments binding of hepatocytes from mice to immobilized plasmin	685347	
3.4.21.7	arachidonate	-	686689	
3.4.21.7	Blood serum	2.0% equine serum increases plasmin activity by ca.50% when assayed with N-Suc-L-Ala-L-Phe-L-Lys-7-amido-4-methyl-coumarin in milk	668957	
3.4.21.7	Efb protein	plasminogen bound to Efb protein is converted to plasmin	732706	
3.4.21.7	Factor IXa	regulates plasmin-catalyzed factor VIIIa inactivation	685399	
3.4.21.7	fragment X	profibrinolytic effect with plasmin. Rates of plasmin formation increase with increasing fragment X concentrations. Plasmin degrades clots containing fragment X more rapidly than fibrin clots	685074	
3.4.21.7	high molecular weight urokinase-type plasminogen activator	induces a significant increase in plasmin activity in unstimulated or lipopolysaccharide-stimulated monocytes	688153	
3.4.21.7	low molecular weight urokinase-type plasminogen activator	induces a significant increase in plasmin activity in unstimulated or lipopolysaccharide-stimulated monocytes	688153	
3.4.21.7	additional information	activation of a low concentration of plasminogen by cell-associated plasminogen activators produces sufficient active plasmin to rapidly and efficiently process pro-brain-derived neurotrophic factor in the pericellular environment	686775	
3.4.21.7	additional information	ATF-urokinase-type plasminogen activator causes little, if any, increase in plasmin activity in unstimulated or lipopolysaccharide-stimulated monocytes	688153	
3.4.21.7	additional information	Glu-plasminogen incubated with adherent cells, i.e. CHO-K1, HEK-293 and HMEC-1 cells, is converted into plasmin for activation by constitutively expressed tPA, i.e. tissue-type plasminogen activator, or uPA, i.e. urokinase-type plasminogen activator	717216	
3.4.21.7	additional information	staphylokinase, SAK, forms a 1:1 stoichiometric complex with human plasmin and switches its substrate specificity to generate a plasminogen activator complex with a crucial requirement of a positively charged and an aromatic residue, respectively, at positions 43 and 44, i.e. SAKHis43 and SAKTyr44, for optimal functioning of SAK-Pm activator complex. Role of these residues in making cation-pi and pi-pi interactions with Trp215 of plasmin and thus establishing the crucial intermolecular contacts within the active site cleft of the activator complex for the cofactor activity of staphylokinase. Molecular modeling and structure analysis, overview	717604	
3.4.21.7	additional information	the increased activity of plasmin after diafiltration may be also due to elimination of small enzyme inhibitor proteins	717666	
3.4.21.7	additional information	the main physiological activators of plasminogen are tissue-type plasminogen activator, which is mainly involved in the dissolution of the fibrin polymers by plasmin, and urokinase-type plasminogen activator, which is primarily responsible for the generation of plasmin activity in the intercellular space. Both activators are multidomain serine proteases	717469	
3.4.21.7	oleate	-	686689	
3.4.21.7	Sbi protein	plasminogen bound to Sbi protein is converted to plasmin	732706	
3.4.21.7	stearate	-	686689	
3.4.21.7	tissue plasminogen activator	-	732241, 753072	
3.4.21.7	urokinase plasminogen activator	-	753072	
3.4.21.7	urokinase plasminogen activator1	-	732241	
3.4.21.7	urokinase-type plasminogen activator	-	732706	
3.4.21.7	urokinase-type plasminogen activator	cleaves plasminogen to give active plasmin	717845	
3.4.21.7	urokinase-type plasminogen activator	converts plasminogen bound to a plasminogen receptor into plasmin	731653	
3.4.21.7	urokinase-type plasminogen activator	plasminogen bound to immunoglobulin-like proteins LigA and LigB is converted to proteolytic active plasmin in the presence of urokinase-type plasminogen activator	753781