PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1692742-1	1990	The catalytic function of catalase and its peroxidatic activity during tetramethylbenzidine (TMB) oxidation by cumene hydroperoxide were studied in reversed micelles of Aerosol OT (AOT) in octane relative to the [H2O]/[AOT] ratio and the initial catalase concentration.	3,3',5,5'-tetramethylbenzidine	71-91	catalase	Homo sapiens	26-34	
8998290-5	1996	In reversed AOT micelles, catalase partially dissociates to subunits because their peroxidase activity was demonstrable in cumene hydroperoxide-dependent oxidation of tetramethylbenzidine.	3,3',5,5'-tetramethylbenzidine	167-187	catalase	Homo sapiens	26-34	
1692742-1	1990	The catalytic function of catalase and its peroxidatic activity during tetramethylbenzidine (TMB) oxidation by cumene hydroperoxide were studied in reversed micelles of Aerosol OT (AOT) in octane relative to the [H2O]/[AOT] ratio and the initial catalase concentration.	3,3',5,5'-tetramethylbenzidine	93-96	catalase	Homo sapiens	26-34	
23806145-4	2013	The carried catalase, followed by the sandwiched immunocomplex, partially consumed the added hydrogen peroxide in the detection solution, which slowed down the catalytic efficiency of magnetic bead-based peroxidase mimics toward TMB/H2O2, thereby weakening the visible color and decreasing the colorimetric density.	3,3',5,5'-tetramethylbenzidine	229-232	catalase	Homo sapiens	12-20