PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20198919-6	2010	Bovine LPO showed high antibacterial activity in 100 mM thiocyanate-100 mM H2O2 medium for some bacteria (Brevibacillus centrosaurus, B. choshinensis, B. lyticum, Cedecea davisae, Chryseobacterium indoltheticum, Clavibacter michiganense pv.	thiocyanate	56-67	lactoperoxidase	Bos taurus	7-10	
32856529-3	2022	In metabolism, LPO has ability to catalyze the transformation of thiocyanate (SCN-) to hypothiocyanite (OSCN-) that is an antibacterial agent and the reaction occurs with hydrogen peroxide.	thiocyanate	65-76	lactoperoxidase	Bos taurus	15-18	
22612925-1	2012	Lactoperoxidase (LP) is the second most abundant enzyme in bovine milk and has been used in conjunction with hydrogen peroxide (H2O2) and thiocyanate (SCN-) to work as an antimicrobial in raw milk where pasteurization is not feasible.	thiocyanate	138-149	lactoperoxidase	Bos taurus	0-15	
22886082-1	2012	Lactoperoxidase (LPO) is a hemeprotein catalyzing the oxidation of thiocyanate and I(-) into antimicrobials and small aromatic organics after being itself oxidized by H(2)O(2).	thiocyanate	67-78	lactoperoxidase	Bos taurus	0-15	
22886082-1	2012	Lactoperoxidase (LPO) is a hemeprotein catalyzing the oxidation of thiocyanate and I(-) into antimicrobials and small aromatic organics after being itself oxidized by H(2)O(2).	thiocyanate	67-78	lactoperoxidase	Bos taurus	17-20	
20198919-9	2010	LPO system has inhibition effects on all type bacteria and concentration is really important such as LPO-100 mM thiocyanate-100 mM H2O2 system was proposed as an effective agent against many factors causing several diseases.	thiocyanate	112-123	lactoperoxidase	Bos taurus	0-3	
20198919-9	2010	LPO system has inhibition effects on all type bacteria and concentration is really important such as LPO-100 mM thiocyanate-100 mM H2O2 system was proposed as an effective agent against many factors causing several diseases.	thiocyanate	112-123	lactoperoxidase	Bos taurus	101-104	
19167310-4	2009	Samples of bovine lactoperoxidase containing thiocyanate (SCN(-)) and hypothiocyanate (OSCN(-)) ions were purified and crystallized.	thiocyanate	45-56	lactoperoxidase	Bos taurus	18-33	
12369411-10	2002	Therefore the exogenous supply of thiocyanate and hydrogen peroxide needed to activate the lactoperoxidase system for raw milk preservation will vary in quantity depending on these factors.	thiocyanate	34-45	lactoperoxidase	Bos taurus	91-106	
8388915-5	1993	Lactoperoxidase complexes with nitrite ion and thiocyanate ion were characterized for comparison with the cyanide complex.	thiocyanate	47-58	lactoperoxidase	Bos taurus	0-15	
8388915-7	1993	Interaction of lactoperoxidase with thiocyanate ion was monitored by NMR and EPR spectroscopy.	thiocyanate	36-47	lactoperoxidase	Bos taurus	15-30	
8388915-8	1993	Proton NMR spectra of lactoperoxidase in the presence of excess thiocyanate ion illustrated the retention of a high-spin ferric configuration consistent with predominant binding of the physiological thiocyanate substrate at a non-heme site at room temperature.	thiocyanate	64-75	lactoperoxidase	Bos taurus	22-37	
8388915-8	1993	Proton NMR spectra of lactoperoxidase in the presence of excess thiocyanate ion illustrated the retention of a high-spin ferric configuration consistent with predominant binding of the physiological thiocyanate substrate at a non-heme site at room temperature.	thiocyanate	199-210	lactoperoxidase	Bos taurus	22-37	
8388915-9	1993	However, EPR spectroscopy at cryogenic temperatures revealed the existence of a low-spin lactoperoxidase thiocyanate complex.	thiocyanate	105-116	lactoperoxidase	Bos taurus	89-104