PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2933077-2	1985	Values of kinetic parameters for the hydrolysis of esters and p-nitroanilides of L-lysine and L-arginine catalyzed by the Lys77 form of human plasmin (EC 3.4.21.7) have been determined between pH 5.5 and 8 (I = 0.1 M) at 21 +/- 0.5 degrees C. Over the whole pH range explored, Lys77-plasmin catalysis conforms to simple Michaelis-Menten kinetics, and steady-state and pre-steady-state data may be consistently fitted to the minimum three-step mechanism: E + S in equilibrium (k+1/k-1)E X S----(k+2)E X P + P1----(k+3)E + P2 In spite of the higher specificity of lysyl derivatives for Lys77-plasmin rather than the arginyl ones, kinetic parameters also depend on the nature of the N-alpha substituent and/or of the alcoholic or p-nitroanilidic moiety of the substrate.	Esters	51-57	plasminogen	Homo sapiens	142-149	
9613812-7	1997	FTIR transmittance spectra confirm microsphere incorporation within the polyurethane tubes and PLG ester hydrolysis occurring over the 3-month period.	Esters	99-104	plasminogen	Homo sapiens	95-98	
8019515-0	1994	Inhibition of trypsin, plasmin, thrombin and kallikrein by various esters of guanidino- and amidino-acids.	Esters	67-73	plasminogen	Homo sapiens	23-30	
2933077-2	1985	Values of kinetic parameters for the hydrolysis of esters and p-nitroanilides of L-lysine and L-arginine catalyzed by the Lys77 form of human plasmin (EC 3.4.21.7) have been determined between pH 5.5 and 8 (I = 0.1 M) at 21 +/- 0.5 degrees C. Over the whole pH range explored, Lys77-plasmin catalysis conforms to simple Michaelis-Menten kinetics, and steady-state and pre-steady-state data may be consistently fitted to the minimum three-step mechanism: E + S in equilibrium (k+1/k-1)E X S----(k+2)E X P + P1----(k+3)E + P2 In spite of the higher specificity of lysyl derivatives for Lys77-plasmin rather than the arginyl ones, kinetic parameters also depend on the nature of the N-alpha substituent and/or of the alcoholic or p-nitroanilidic moiety of the substrate.	Esters	51-57	plasminogen	Homo sapiens	283-290	
2933077-2	1985	Values of kinetic parameters for the hydrolysis of esters and p-nitroanilides of L-lysine and L-arginine catalyzed by the Lys77 form of human plasmin (EC 3.4.21.7) have been determined between pH 5.5 and 8 (I = 0.1 M) at 21 +/- 0.5 degrees C. Over the whole pH range explored, Lys77-plasmin catalysis conforms to simple Michaelis-Menten kinetics, and steady-state and pre-steady-state data may be consistently fitted to the minimum three-step mechanism: E + S in equilibrium (k+1/k-1)E X S----(k+2)E X P + P1----(k+3)E + P2 In spite of the higher specificity of lysyl derivatives for Lys77-plasmin rather than the arginyl ones, kinetic parameters also depend on the nature of the N-alpha substituent and/or of the alcoholic or p-nitroanilidic moiety of the substrate.	Esters	51-57	plasminogen	Homo sapiens	283-290	
6214801-2	1982	The inhibitory effect of esters of N-alpha-arylsulfonyl-4-amidinophenylalanine against trypsin, plasmin and thrombin].	Esters	25-31	plasminogen	Homo sapiens	96-103	
38847-3	1979	The reactions of plasmin and trypsin with p-nitroanilides show kc values similar to those normally found with specific ester substrates, indicating that the deacylation steps of the reactions are rate determining.	Esters	119-124	plasminogen	Homo sapiens	17-24	
4228923-2	1967	Serum plasmin activity in the normal subject by the ester analysis method].	Esters	52-57	plasminogen	Homo sapiens	6-13