PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8300211-0 1994 Antibacterial activity of hydrogen peroxide and the lactoperoxidase-hydrogen peroxide-thiocyanate system against oral streptococci. thiocyanate 86-97 lactoperoxidase Homo sapiens 52-67 10191475-1 1999 The lactoperoxidase system is a naturally occurring antimicrobial system found in milk, with lactoperoxidase, thiocyanate and hydrogen peroxide as its components. thiocyanate 110-121 lactoperoxidase Homo sapiens 4-19 8300211-1 1994 In secreted fluids, the enzyme lactoperoxidase (LP) catalyzes the oxidation of thiocyanate ion (SCN-) by hydrogen peroxide (H2O2), producing the weak oxidizing agent hypothiocyanite (OSCN-), which has bacteriostatic activity. thiocyanate 79-90 lactoperoxidase Homo sapiens 31-46 8300211-1 1994 In secreted fluids, the enzyme lactoperoxidase (LP) catalyzes the oxidation of thiocyanate ion (SCN-) by hydrogen peroxide (H2O2), producing the weak oxidizing agent hypothiocyanite (OSCN-), which has bacteriostatic activity. thiocyanate 79-90 lactoperoxidase Homo sapiens 48-50 8300211-1 1994 In secreted fluids, the enzyme lactoperoxidase (LP) catalyzes the oxidation of thiocyanate ion (SCN-) by hydrogen peroxide (H2O2), producing the weak oxidizing agent hypothiocyanite (OSCN-), which has bacteriostatic activity. thiocyanate 96-99 lactoperoxidase Homo sapiens 31-46 8300211-1 1994 In secreted fluids, the enzyme lactoperoxidase (LP) catalyzes the oxidation of thiocyanate ion (SCN-) by hydrogen peroxide (H2O2), producing the weak oxidizing agent hypothiocyanite (OSCN-), which has bacteriostatic activity. thiocyanate 96-99 lactoperoxidase Homo sapiens 48-50 1390933-0 1992 Lactoperoxidase-catalyzed oxidation of thiocyanate ion: a carbon-13 nuclear magnetic resonance study of the oxidation products. thiocyanate 39-50 lactoperoxidase Homo sapiens 0-15 8501464-0 1993 NMR relaxation studies of the interaction of thiocyanate with lactoperoxidase. thiocyanate 45-56 lactoperoxidase Homo sapiens 62-77 8501464-1 1993 The interaction of lactoperoxidase, LPO, with its substrate, thiocyanate, SCN-, has been investigated by 13C and 15N NMR relaxation measurements. thiocyanate 61-72 lactoperoxidase Homo sapiens 19-34 8501464-1 1993 The interaction of lactoperoxidase, LPO, with its substrate, thiocyanate, SCN-, has been investigated by 13C and 15N NMR relaxation measurements. thiocyanate 61-72 lactoperoxidase Homo sapiens 36-39 8501464-2 1993 When 0.1 M SCN-, enriched with either 13C or 15N, was titrated with native ferric lactoperoxidase a large change in the spin-lattice relaxation time of the respective nucleus was observed. thiocyanate 11-14 lactoperoxidase Homo sapiens 82-97 8501464-7 1993 Apparent distances between the heme iron of lactoperoxidase and either the carbon or nitrogen atoms of bound thiocyanate ion have been determined through application of the Solomon-Bloembergen equation. thiocyanate 109-120 lactoperoxidase Homo sapiens 44-59 1390933-1 1992 Products formed from the lactoperoxidase (LPO) catalyzed oxidation of thiocyanate ion (SCN-) with hydrogen peroxide (H2O2) have been studied by 13C-NMR at pH 6 and pH 7. thiocyanate 70-81 lactoperoxidase Homo sapiens 25-40 1390933-1 1992 Products formed from the lactoperoxidase (LPO) catalyzed oxidation of thiocyanate ion (SCN-) with hydrogen peroxide (H2O2) have been studied by 13C-NMR at pH 6 and pH 7. thiocyanate 70-81 lactoperoxidase Homo sapiens 42-45 2154109-1 1990 Salivary peroxidase and to a lesser extent myeloperoxidase are present in significant concentrations in saliva and catalyze the oxidation of thiocyanate anion (SCN-) by H2O2 to yield the potent oxidants hypothiocyanous acid (HOSCN) and its conjugate base hypothiocyanite anion (OSCN-). thiocyanate 141-158 lactoperoxidase Homo sapiens 0-19 2154109-1 1990 Salivary peroxidase and to a lesser extent myeloperoxidase are present in significant concentrations in saliva and catalyze the oxidation of thiocyanate anion (SCN-) by H2O2 to yield the potent oxidants hypothiocyanous acid (HOSCN) and its conjugate base hypothiocyanite anion (OSCN-). thiocyanate 160-163 lactoperoxidase Homo sapiens 0-19 34761444-2 2022 To perform it"s innate immune action against invading microbes, LPO utilizes hydrogen peroxide (H2 O2 ) to convert thiocyanate (SCN ) and iodide (I ) ions into the oxidizing compounds hypothiocyanite (OSCN ) and hypoiodite (IO ). thiocyanate 115-126 lactoperoxidase Homo sapiens 64-67 6724690-1 1984 Lactoperoxidase catalyzes the oxidation of thiocyanate by hydrogen peroxide into hypothiocyanite, a reaction which can protect bacterial and mammalian cells from killing by hydrogen peroxide. thiocyanate 43-54 lactoperoxidase Homo sapiens 0-15 34829517-1 2021 Lactoperoxidase (LPO, FeIII in its resting state in the absence of substrates)-an enzyme secreted from human mammary, salivary, and other mucosal glands-catalyzes the oxidation of thiocyanate (SCN-) by hydrogen peroxide (H2O2) to produce hypothiocyanite (OSCN-), which functions as an antimicrobial agent. thiocyanate 180-191 lactoperoxidase Homo sapiens 0-15 34829517-1 2021 Lactoperoxidase (LPO, FeIII in its resting state in the absence of substrates)-an enzyme secreted from human mammary, salivary, and other mucosal glands-catalyzes the oxidation of thiocyanate (SCN-) by hydrogen peroxide (H2O2) to produce hypothiocyanite (OSCN-), which functions as an antimicrobial agent. thiocyanate 180-191 lactoperoxidase Homo sapiens 17-20 2826736-5 1987 In saliva the most important part of this defense is salivary peroxidase, which detoxifies hydrogen peroxide in the presence of thiocyanate by converting it into hypothiocyanite, dioxygen and water. thiocyanate 128-139 lactoperoxidase Homo sapiens 53-72 2826737-2 1987 If the oxidation of thiocyanate (which occurs, in vivo, in human saliva and salivary glands) is a vital reaction for the maintenance of oral health, then the enzyme (salivary peroxidase), which catalyzes this reaction, should function optimally under in vivo conditions. thiocyanate 20-31 lactoperoxidase Homo sapiens 166-185 2548589-0 1989 Binding of thiocyanate to lactoperoxidase: 1H and 15N nuclear magnetic resonance studies. thiocyanate 11-22 lactoperoxidase Homo sapiens 26-41 2548589-1 1989 The binding of thiocyanate to lactoperoxidase (LPO) has been investigated by 1H and 15N NMR spectroscopy. thiocyanate 15-26 lactoperoxidase Homo sapiens 30-45 2548589-1 1989 The binding of thiocyanate to lactoperoxidase (LPO) has been investigated by 1H and 15N NMR spectroscopy. thiocyanate 15-26 lactoperoxidase Homo sapiens 47-50 2548589-2 1989 1H NMR of LPO shows that the major broad heme methyl proton resonance at about 61 ppm is shifted upfield by addition of the thiocyanate, indicating binding of the thiocyanate to the enzyme. thiocyanate 124-135 lactoperoxidase Homo sapiens 10-13 2548589-2 1989 1H NMR of LPO shows that the major broad heme methyl proton resonance at about 61 ppm is shifted upfield by addition of the thiocyanate, indicating binding of the thiocyanate to the enzyme. thiocyanate 163-174 lactoperoxidase Homo sapiens 10-13 2548589-6 1989 The thiocyanate is shown to bind at the same site of LPO as iodide does, but the binding is considerably weaker and is away from the ferric ion. thiocyanate 4-15 lactoperoxidase Homo sapiens 53-56 3349029-0 1988 Steady-state kinetics of thiocyanate oxidation catalyzed by human salivary peroxidase. thiocyanate 25-36 lactoperoxidase Homo sapiens 66-85 3349029-5 1988 The pH-independent second-order rate constants (k4) for the oxidation of thiocyanate by compound I were estimated to be 5 X 10(6) M-1 s-1 (SD = 1, n = 18) for LPO and 9 X 10(6) M-1 s-1 (SD = 2, n = 11) for SPO. thiocyanate 73-84 lactoperoxidase Homo sapiens 159-162 2837167-8 1988 We conclude that most of the hydrogen cyanide found in breath from normal human beings originates from oxidation of thiocyanate by salivary peroxidase in the oropharynx. thiocyanate 116-127 lactoperoxidase Homo sapiens 131-150 6724690-2 1984 The present study demonstrates, however, that lactoperoxidase in the presence of thiocyanate can actually potentiate the bactericidal and cytotoxic effects of hydrogen peroxide under specific conditions, such as when hydrogen peroxide is present in the reaction mixtures in excess of thiocyanate. thiocyanate 81-92 lactoperoxidase Homo sapiens 46-61 6724690-2 1984 The present study demonstrates, however, that lactoperoxidase in the presence of thiocyanate can actually potentiate the bactericidal and cytotoxic effects of hydrogen peroxide under specific conditions, such as when hydrogen peroxide is present in the reaction mixtures in excess of thiocyanate. thiocyanate 284-295 lactoperoxidase Homo sapiens 46-61 6686988-7 1983 The rate of acid production of the cells in the presence of glucose was inhibited, however, by the combination lactoperoxidase-thiocyanate-hydrogen peroxide. thiocyanate 127-138 lactoperoxidase Homo sapiens 111-126 6651827-1 1983 Lactoperoxidase catalyzed the catalatic decomposition of H2O2 in the presence of SCN-. thiocyanate 81-84 lactoperoxidase Homo sapiens 0-15 5449131-2 1970 Lactoperoxidase (EC 1.11.1.7), an enzyme present in various mammalian glands and in their secretions, catalyses the oxidation of thiocyanate by hydrogen peroxide to form a compound that inhibits the growth, oxygen uptake and acid production of certain bacteria. thiocyanate 129-140 lactoperoxidase Homo sapiens 0-15 7033135-3 1982 The products of the reaction between hydrogen peroxide and thiocyanate in the presence of lactoperoxidase were not bactericidal except in the case of E. coli, and then only under special conditions. thiocyanate 59-70 lactoperoxidase Homo sapiens 90-105 299018-0 1978 Salivary peroxidase activity and thiocyanate concentration in human subjects with genetic variants of salivary peroxidase. thiocyanate 33-44 lactoperoxidase Homo sapiens 102-121 4317722-1 1970 Lactoperoxidase (EC 1.11.1.7) catalysed the oxidation of NADH by hydrogen peroxide in the presence of either thiocyanate, iodide or bromide. thiocyanate 109-120 lactoperoxidase Homo sapiens 0-15 6295491-0 1982 The peroxidation of thiocyanate catalysed by myeloperoxidase and lactoperoxidase. thiocyanate 20-31 lactoperoxidase Homo sapiens 65-80 6295491-1 1982 Peroxidation of SCN- to OSCN-, catalysed by myeloperoxidase and lactoperoxidase, was studied. thiocyanate 16-19 lactoperoxidase Homo sapiens 64-79 7066307-0 1982 Lactoperoxidase-catalyzed oxidation of thiocyanate: polarographic study of the oxidation products. thiocyanate 39-50 lactoperoxidase Homo sapiens 0-15 7066307-1 1982 The lactoperoxidase-catalyzed oxidation of thiocyanate (SCN-) was studied by two different polarographic techniques: direct current polarography and linear sweep voltammetry. thiocyanate 43-54 lactoperoxidase Homo sapiens 4-19 7066307-10 1982 This new peak may represent higher oxy acids of SCN- (O2SCN-, O3SCN-), formed in the oxidation of OSCN- by H2O2 or by H2O2-LPO. thiocyanate 48-51 lactoperoxidase Homo sapiens 123-126 7248282-0 1981 Lactoperoxidase-catalyzed oxidation of thiocyanate: equilibria between oxidized forms of thiocyanate. thiocyanate 39-50 lactoperoxidase Homo sapiens 0-15 7248282-0 1981 Lactoperoxidase-catalyzed oxidation of thiocyanate: equilibria between oxidized forms of thiocyanate. thiocyanate 89-100 lactoperoxidase Homo sapiens 0-15 7248302-6 1981 When H2O2 and SCN- were applied to a Sepharose column bearing covalently attached lactoperoxidase, the column eluate inactivated hexokinase. thiocyanate 14-17 lactoperoxidase Homo sapiens 82-97 413849-1 1978 Activation of the antibacterial lactoperoxidase system in milk, i.e. increasing the thiocyanate concentration to 0.25 mM and adding an equimolar amount of H2O2, results in a substantial reduction of the bacterial flora and prevents the multiplication of psychrotrophic bacteria for up to 5 d. This treatment has no effect on the physico-chemical properties of milk and does not lead to the accumulation of resistant bacteria. thiocyanate 84-95 lactoperoxidase Homo sapiens 32-47 911776-0 1977 Lactoperoxidase-catalyzed incorporation of thiocyanate ion into a protein substrate. thiocyanate 43-54 lactoperoxidase Homo sapiens 0-15 30202407-3 2018 In saliva, LPO catalyzes the hydrogen peroxide-dependent oxidation of thiocyanate to hypothiocyanite that exhibits antimicrobial and antiviral properties. thiocyanate 70-81 lactoperoxidase Homo sapiens 11-14 33882424-1 2021 Lactoperoxidase (LPO) is a mammalian heme peroxidase which catalyzes the conversion of thiocyanate (SCN ) and iodide (I-) by hydrogen peroxide (H2O2) into antimicrobial hypothiocyanite (OSCN ) and hypoiodite (IO-). thiocyanate 87-98 lactoperoxidase Homo sapiens 0-15 33882424-1 2021 Lactoperoxidase (LPO) is a mammalian heme peroxidase which catalyzes the conversion of thiocyanate (SCN ) and iodide (I-) by hydrogen peroxide (H2O2) into antimicrobial hypothiocyanite (OSCN ) and hypoiodite (IO-). thiocyanate 87-98 lactoperoxidase Homo sapiens 17-20 31734539-2 2020 Lactoperoxidase is a hemoprotein that utilizes hydrogen peroxide (H2O2) and thiocyanate (SCN-) to produce hypothiocyanous acid (HOSCN), an antimicrobial agent also thought to be associated with carcinogenesis. thiocyanate 76-87 lactoperoxidase Homo sapiens 0-15 33152878-2 2021 The traditional method for LPO activity measurement using ABTS (2,2"-azinobis(3-ethylbenzothiazoline-6-sulphonate) cannot achieve high sensitivity and is affected by indigenous milk thiocyanate. thiocyanate 182-193 lactoperoxidase Homo sapiens 27-30 33152878-4 2021 The assay is particularly suitable for milk LPO activity measurement as it eliminates the influences of indigenous milk hydrogen peroxide and thiocyanate. thiocyanate 142-153 lactoperoxidase Homo sapiens 44-47 30876918-5 2019 LPO utilizes hydrogen peroxide (H2O2) and the pseudohalide thiocyanate (-SCN) to generate a broad-spectrum antimicrobial oxidant hypothiocyanous acid (HOSCN). thiocyanate 59-70 lactoperoxidase Homo sapiens 0-3 30876918-5 2019 LPO utilizes hydrogen peroxide (H2O2) and the pseudohalide thiocyanate (-SCN) to generate a broad-spectrum antimicrobial oxidant hypothiocyanous acid (HOSCN). thiocyanate 72-76 lactoperoxidase Homo sapiens 0-3 24928513-10 2014 At physiologically relevant concentrations, urate competed effectively with thiocyanate, the main substrate of LPO for oxidation, and inhibited production of hypothiocyanite. thiocyanate 76-87 lactoperoxidase Homo sapiens 111-114 29032047-1 2018 OBJECTIVES: The enzyme lactoperoxidase (LPO), which is released into several body fluids like saliva, is an essential part to maintain the oral bacterial homeostasis by catalysing the oxidation of thiocyanate (SCN-) to hypo-thiocyanite (-OSCN). thiocyanate 197-208 lactoperoxidase Homo sapiens 40-43 29032047-1 2018 OBJECTIVES: The enzyme lactoperoxidase (LPO), which is released into several body fluids like saliva, is an essential part to maintain the oral bacterial homeostasis by catalysing the oxidation of thiocyanate (SCN-) to hypo-thiocyanite (-OSCN). thiocyanate 210-213 lactoperoxidase Homo sapiens 40-43 28653416-2 2017 LPO catalyzes the oxidation of a number of substrates including thiocyanate while TPO catalyzes the biosynthesis of thyroid hormones. thiocyanate 64-75 lactoperoxidase Homo sapiens 0-3 26558497-3 2016 The generation of oxidized thiocyanate and/or iodine species is also important in numerous biotechnological applications of LPO. thiocyanate 27-38 lactoperoxidase Homo sapiens 124-127 30472870-1 2018 Hypothiocyanite (OSCN-) is a natural component of human saliva and is produced by the lactoperoxidase (LPO)/thiocyanate/hydrogen peroxide (H2O2) system. thiocyanate 108-119 lactoperoxidase Homo sapiens 86-101 30472870-1 2018 Hypothiocyanite (OSCN-) is a natural component of human saliva and is produced by the lactoperoxidase (LPO)/thiocyanate/hydrogen peroxide (H2O2) system. thiocyanate 108-119 lactoperoxidase Homo sapiens 103-106 29272487-3 2017 Thiocyanate reacts with H2O2 in the presence of lactoperoxidase (LPO) to form hypothiocyanate (OSCN-), which acts as a biocide and H2O2 scavenging system to reduce damage during inflammation. thiocyanate 0-11 lactoperoxidase Homo sapiens 48-63 29272487-3 2017 Thiocyanate reacts with H2O2 in the presence of lactoperoxidase (LPO) to form hypothiocyanate (OSCN-), which acts as a biocide and H2O2 scavenging system to reduce damage during inflammation. thiocyanate 0-11 lactoperoxidase Homo sapiens 65-68 25772156-6 2015 Functionally, LPO is a crucial component of the LPO system that includes LPO, hydrogen peroxide (H2O2), and thiocyanate (SCN(-)), being a well-studied, naturally occurring antimicrobial system in milk that is effective against many microorganisms and some viruses. thiocyanate 108-119 lactoperoxidase Homo sapiens 14-17 25772156-6 2015 Functionally, LPO is a crucial component of the LPO system that includes LPO, hydrogen peroxide (H2O2), and thiocyanate (SCN(-)), being a well-studied, naturally occurring antimicrobial system in milk that is effective against many microorganisms and some viruses. thiocyanate 108-119 lactoperoxidase Homo sapiens 48-51 25772156-6 2015 Functionally, LPO is a crucial component of the LPO system that includes LPO, hydrogen peroxide (H2O2), and thiocyanate (SCN(-)), being a well-studied, naturally occurring antimicrobial system in milk that is effective against many microorganisms and some viruses. thiocyanate 108-119 lactoperoxidase Homo sapiens 48-51 25772156-6 2015 Functionally, LPO is a crucial component of the LPO system that includes LPO, hydrogen peroxide (H2O2), and thiocyanate (SCN(-)), being a well-studied, naturally occurring antimicrobial system in milk that is effective against many microorganisms and some viruses. thiocyanate 121-124 lactoperoxidase Homo sapiens 14-17 25772156-6 2015 Functionally, LPO is a crucial component of the LPO system that includes LPO, hydrogen peroxide (H2O2), and thiocyanate (SCN(-)), being a well-studied, naturally occurring antimicrobial system in milk that is effective against many microorganisms and some viruses. thiocyanate 121-124 lactoperoxidase Homo sapiens 48-51 25772156-6 2015 Functionally, LPO is a crucial component of the LPO system that includes LPO, hydrogen peroxide (H2O2), and thiocyanate (SCN(-)), being a well-studied, naturally occurring antimicrobial system in milk that is effective against many microorganisms and some viruses. thiocyanate 121-124 lactoperoxidase Homo sapiens 48-51 24928513-0 2014 Uric acid and thiocyanate as competing substrates of lactoperoxidase. thiocyanate 14-25 lactoperoxidase Homo sapiens 53-68 24928513-4 2014 LPO is a mammalian peroxidase that plays a key role in the innate immune defense by oxidizing thiocyanate to the bactericidal and fungicidal agent hypothiocyanite. thiocyanate 94-105 lactoperoxidase Homo sapiens 0-3 25309750-6 2014 The last part looks upon the characteristics of the active molecule produced by lactoperoxidase in the presence of thiocyanate and/or iodide with implication(s) on its antimicrobial activity. thiocyanate 115-126 lactoperoxidase Homo sapiens 80-95 24053146-3 2014 The LPO-catalyzed reaction between H2O2 and SCN(-) yields the bactericidal hypothiocyanite (OSCN(-)) in airway surface liquid (ASL). thiocyanate 44-47 lactoperoxidase Homo sapiens 4-7 19705807-3 2009 In the oral cavity, salivary peroxidase and MPO catalyze the oxidation of the pseudohalide thiocyanate (SCN(-)) by hydrogen peroxide to produce the antimicrobial hypothiocyanite (OSCN(-)). thiocyanate 91-102 lactoperoxidase Homo sapiens 20-39 22968041-1 2012 Thiocyanate (SCN) functions in host defense as part of the secreted lactoperoxidase (LPO) microbicidal pathway. thiocyanate 0-11 lactoperoxidase Homo sapiens 68-83 22968041-1 2012 Thiocyanate (SCN) functions in host defense as part of the secreted lactoperoxidase (LPO) microbicidal pathway. thiocyanate 0-11 lactoperoxidase Homo sapiens 85-88 22968041-1 2012 Thiocyanate (SCN) functions in host defense as part of the secreted lactoperoxidase (LPO) microbicidal pathway. thiocyanate 13-16 lactoperoxidase Homo sapiens 68-83 22968041-1 2012 Thiocyanate (SCN) functions in host defense as part of the secreted lactoperoxidase (LPO) microbicidal pathway. thiocyanate 13-16 lactoperoxidase Homo sapiens 85-88 22132121-1 2011 Lactoperoxidase (LPO) is the major consumer of hydrogen peroxide (H(2)O(2)) in the airways through its ability to oxidize thiocyanate (SCN(-)) to produce hypothiocyanous acid, an antimicrobial agent. thiocyanate 122-133 lactoperoxidase Homo sapiens 0-15 22132121-1 2011 Lactoperoxidase (LPO) is the major consumer of hydrogen peroxide (H(2)O(2)) in the airways through its ability to oxidize thiocyanate (SCN(-)) to produce hypothiocyanous acid, an antimicrobial agent. thiocyanate 122-133 lactoperoxidase Homo sapiens 17-20 22132121-1 2011 Lactoperoxidase (LPO) is the major consumer of hydrogen peroxide (H(2)O(2)) in the airways through its ability to oxidize thiocyanate (SCN(-)) to produce hypothiocyanous acid, an antimicrobial agent. thiocyanate 135-138 lactoperoxidase Homo sapiens 0-15 22132121-1 2011 Lactoperoxidase (LPO) is the major consumer of hydrogen peroxide (H(2)O(2)) in the airways through its ability to oxidize thiocyanate (SCN(-)) to produce hypothiocyanous acid, an antimicrobial agent. thiocyanate 135-138 lactoperoxidase Homo sapiens 17-20 19768779-1 2010 Lactoperoxidase (LPO), a mammalian secretory heme peroxidase, catalyzes the oxidation of thiocyanate by hydrogen peroxide to produce hypothiocyanate, an antibacterial agent. thiocyanate 89-100 lactoperoxidase Homo sapiens 0-15 19768779-1 2010 Lactoperoxidase (LPO), a mammalian secretory heme peroxidase, catalyzes the oxidation of thiocyanate by hydrogen peroxide to produce hypothiocyanate, an antibacterial agent. thiocyanate 89-100 lactoperoxidase Homo sapiens 17-20 19918082-5 2009 First, lactoperoxidase (LPO) in the airways catalyzes oxidation of SCN(-) to tissue-innocuous hypothiocyanite (OSCN(-)), while consuming H(2)O(2). thiocyanate 67-70 lactoperoxidase Homo sapiens 24-27 19705807-3 2009 In the oral cavity, salivary peroxidase and MPO catalyze the oxidation of the pseudohalide thiocyanate (SCN(-)) by hydrogen peroxide to produce the antimicrobial hypothiocyanite (OSCN(-)). thiocyanate 104-107 lactoperoxidase Homo sapiens 20-39 17250799-4 2007 The pseudoperoxidase activity of lactoperoxidase increased lipid peroxidation, while thiocyanate and nitrite-reduced lipid peroxidation. thiocyanate 85-96 lactoperoxidase Homo sapiens 33-48 19725235-1 2009 BACKGROUND AND OBJECTIVES: Lactoperoxidase system contains Lactoperoxidase, Hydrogen peroxide and Thiocyanate ions, which have inhibitory action against cariogenic oral microflora. thiocyanate 98-109 lactoperoxidase Homo sapiens 27-42 19725235-8 2009 CONCLUSION: The levels of thiocyanate ions can be increased in vivo by supplementing the saliva with natural enzymes like lactoperoxidase. thiocyanate 26-37 lactoperoxidase Homo sapiens 122-137 19339248-0 2009 Structural evidence of substrate specificity in mammalian peroxidases: structure of the thiocyanate complex with lactoperoxidase and its interactions at 2.4 A resolution. thiocyanate 88-99 lactoperoxidase Homo sapiens 113-128 19339248-1 2009 The crystal structure of the complex of lactoperoxidase (LPO) with its physiological substrate thiocyanate (SCN(-)) has been determined at 2.4A resolution. thiocyanate 95-106 lactoperoxidase Homo sapiens 40-55 19339248-1 2009 The crystal structure of the complex of lactoperoxidase (LPO) with its physiological substrate thiocyanate (SCN(-)) has been determined at 2.4A resolution. thiocyanate 95-106 lactoperoxidase Homo sapiens 57-60 18802092-1 2008 The dual oxidase-thiocyanate-lactoperoxidase (Duox/SCN(-)/LPO) system generates the microbicidal oxidant hypothiocyanite in the airway surface liquid by using LPO, thiocyanate, and Duox-derived hydrogen peroxide released from the apical surface of the airway epithelium. thiocyanate 17-28 lactoperoxidase Homo sapiens 58-61 18802092-1 2008 The dual oxidase-thiocyanate-lactoperoxidase (Duox/SCN(-)/LPO) system generates the microbicidal oxidant hypothiocyanite in the airway surface liquid by using LPO, thiocyanate, and Duox-derived hydrogen peroxide released from the apical surface of the airway epithelium. thiocyanate 17-28 lactoperoxidase Homo sapiens 159-162 17204267-2 2007 Airway host defense depends on lactoperoxidase (LPO) that requires thiocyanate (SCN-) to function and epithelia use CFTR to concentrate SCN- at the apical surface. thiocyanate 67-78 lactoperoxidase Homo sapiens 31-46 17204267-2 2007 Airway host defense depends on lactoperoxidase (LPO) that requires thiocyanate (SCN-) to function and epithelia use CFTR to concentrate SCN- at the apical surface. thiocyanate 67-78 lactoperoxidase Homo sapiens 48-51 17029415-0 2006 Lactoperoxidase-catalyzed oxidation of thiocyanate by hydrogen peroxide: a reinvestigation of hypothiocyanite by nuclear magnetic resonance and optical spectroscopy. thiocyanate 39-50 lactoperoxidase Homo sapiens 0-15 16212035-8 2005 The LPO--100 mM thiocyanate--100 mM H2O2 system was purposed as an effective agent against many of the diseases causing organisms in human and animals. thiocyanate 16-27 lactoperoxidase Homo sapiens 4-7 12269834-0 2002 Reaction of lactoperoxidase compound I with halides and thiocyanate. thiocyanate 56-67 lactoperoxidase Homo sapiens 12-27 16277530-2 2005 The mammalian peroxidases eosinophil peroxidase, lactoperoxidase (LPO), and myeloperoxidase oxidize thiocyanate to the antimicrobial agents hypothiocyanous acid (HOSCN) and (SCN)2 and are part of a defense system that protects the host from infections. thiocyanate 100-111 lactoperoxidase Homo sapiens 49-64 16277530-2 2005 The mammalian peroxidases eosinophil peroxidase, lactoperoxidase (LPO), and myeloperoxidase oxidize thiocyanate to the antimicrobial agents hypothiocyanous acid (HOSCN) and (SCN)2 and are part of a defense system that protects the host from infections. thiocyanate 100-111 lactoperoxidase Homo sapiens 66-69 16277530-10 2005 In contrast, oxidation by LPO of thiocyanate, the normal substrate of this enzyme, does not result in heme modification. thiocyanate 33-44 lactoperoxidase Homo sapiens 26-29 15894800-1 2005 We investigated the potential role of the co-substrate, thiocyanate (SCN-), in modulating the catalytic activity of myeloperoxidase (MPO) and other members of the mammalian peroxidase superfamily (lactoperoxidase (LPO) and eosinophil peroxidase (EPO)). thiocyanate 56-67 lactoperoxidase Homo sapiens 197-212 15894800-1 2005 We investigated the potential role of the co-substrate, thiocyanate (SCN-), in modulating the catalytic activity of myeloperoxidase (MPO) and other members of the mammalian peroxidase superfamily (lactoperoxidase (LPO) and eosinophil peroxidase (EPO)). thiocyanate 56-67 lactoperoxidase Homo sapiens 214-217 15345749-2 2004 As H(2)O(2) and thiocyanate (SCN(-)) are also present, a functional LPO antibacterial defence system exists in the airways. thiocyanate 16-27 lactoperoxidase Homo sapiens 68-71 15345749-2 2004 As H(2)O(2) and thiocyanate (SCN(-)) are also present, a functional LPO antibacterial defence system exists in the airways. thiocyanate 29-32 lactoperoxidase Homo sapiens 68-71