Salivary peroxidases

Banerjee, Ranajit K.; Datta, Asoke G.

doi:10.1007/bf00233801

Cited by 17 publications

(10 citation statements)

References 71 publications

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“…The first one could represent an inhibition of the enzyme by (i) molecules or proteins and (ii) external conditions such as pH and temperature. For example, cyanide, azide, nitrite, mercaptomethylimidazole, thiourea, superoxide, high levels of nitric oxide, and high levels of thiocyanate bind to the native enzyme and alter Compound I formation [ 20 , 46 , 47 , 52 – 54 ]. With thiocyanate, inhibition is linked to the restriction of the binding site to hydrogen peroxide and the interaction of SCN − with a water molecule [ 23 ].…”

Section: Mode Of Action Of Lactoperoxidasementioning

confidence: 99%

Mode of Action of Lactoperoxidase as Related to Its Antimicrobial Activity: A Review

Bafort

Parisi

Perraudin³

et al. 2014

Enzyme Research

131

141

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Lactoperoxidase is a member of the family of the mammalian heme peroxidases which have a broad spectrum of activity. Their best known effect is their antimicrobial activity that arouses much interest in in vivo and in vitro applications. In this context, the proper use of lactoperoxidase needs a good understanding of its mode of action, of the factors that favor or limit its activity, and of the features and properties of the active molecules. The first part of this review describes briefly the classification of mammalian peroxidases and their role in the human immune system and in host cell damage. The second part summarizes present knowledge on the mode of action of lactoperoxidase, with special focus on the characteristics to be taken into account for in vitro or in vivo antimicrobial use. 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.

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Section: Mode Of Action Of Lactoperoxidasementioning

confidence: 99%

Mode of Action of Lactoperoxidase as Related to Its Antimicrobial Activity: A Review

Bafort

Parisi

Perraudin³

et al. 2014

Enzyme Research

131

141

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“…Both soluble and membrane-bound peroxidases (donor-H # O # oxidoreductase, EC 1.11.1.7) having a wide range of biological functions are present in animal tissues [1,2]. Apart from thyroid peroxidase, they take part in either antibacterial actions or cellular defence against oxidative damage by reactive oxygen species.…”

Section: Introductionmentioning

confidence: 99%

Characterization of sheep lacrimal-gland peroxidase and its major physiological electron donor

Mazumdar

Chatterjee

Adak

et al. 1996

Biochemical Journal

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A soluble sheep lacrimal-gland peroxidase was purified to apparent homogeneity. It had a native molecular mass of 75 kDa with a subunit molecular mass of 82 kDa and an isoelectric point of 6.5. Western blotting showed that it shares some of the enzyme antigenic determinants in common with other soluble peroxidases. The enzyme exhibits a Soret peak at 410 nm which is shifted to 431 nm by 5 equiv. of H2O2 due to the formation of compound II. The latter is, however, unstable and gradually returns to the native state. The enzyme forms complexes with CN- and N3- and is reduced by dithionite showing a characteristic reduced peroxidase spectrum. Although the enzyme oxidizes I-, SCN- and Br- optimally at pH 5.5., 5.25 and 5.0 respectively, at physiological pH, it oxidizes I- and SCN- only. Since extracellular SCN- concentration is much higher than I-, SCN- may act as the major electron donor to the enzyme. The second-order rate constants for the reaction of the enzyme with H2O2 (k+1) and of compound I with SCN- (k+2) were 4 X 10(7) M-1 X s-1 and 8.1 X 10(5) M-1 X s-1 respectively. A plot of log Vmax against pH yields a sigmoidal curve consistent with a single ionizable group on the enzyme with a pK(a) value of 5.75, controlling thiocyanate oxidation. In a coupled system with the peroxidase, H2O2, SCN-, GSH, NADPH and glutathione reductase, peroxidase-catalysed SCN- oxidation by H2O2 could be coupled to NADPH consumption. The system is proposed to operate in vivo for the efficient elimination of endogenous H2O2.

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“…The presence of electrolytes in saliva may have affected the solubility of AMS. Measuring peroxidases in saliva [13] for kinetics of oxidation of AMS to AMSO and AMSO2 may have clarified breakdown products present. It is possible that these highly volatile compounds may be more readily detectable using a solid phase micro-extraction GC-MS, or headspace analysis methodology [14][15][16].…”

Section: Resultsmentioning

confidence: 99%

Attempt to Detect Garlic Allyl Sulphides from Saliva after Consumption of Garlic Tablets Using GC-MS

Watson

Souza²,

Silva³

et al. 2013

J Microb Biochem Technol

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Allicin is an organosulfur compound of Allium sativum (garlic) with anti-fungal and antimicrobial properties. However, to date, neither allicin nor its metabolites has been detected in human organs or bodily fluids following oral consumption of garlic. Bioavailability has only been demonstrated using breath studies. Enteric-coated formulations are designed to pass through the acidic stomach environment; hence detection of garlic compounds in saliva following consumption of enteric-coated garlic tablets would provide evidence of bioavailability in a body secretion. An attempt was made to identify metabolites dially disulphide and allyl methyl sulphide using Gas Chromatography Mass Spectrometry (GC-MS). We completed a single participant mass spectrometry study using 13 time points over 24 hours following consumption of 20 enteric-coated garlic tablets. There was no detection of allicin derived sulfides at any time point. In summary, it is possible that these highly volatile compounds may be more readily detectable using a solid phase micro-extraction GC-MS, or headspace analysis methodology, although the less volatile allyl methyl sulfone and allyl methyl sulfoxide may be the main metabolites present.

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Salivary peroxidases

Cited by 17 publications

References 71 publications

Mode of Action of Lactoperoxidase as Related to Its Antimicrobial Activity: A Review

Mode of Action of Lactoperoxidase as Related to Its Antimicrobial Activity: A Review

Characterization of sheep lacrimal-gland peroxidase and its major physiological electron donor

Attempt to Detect Garlic Allyl Sulphides from Saliva after Consumption of Garlic Tablets Using GC-MS

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