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Horseradish peroxidase is a 44,173.9-dalton glycoprotein with six lysine residues which can be conjugated to a labeled molecule. It produces a coloured, fluorimetric [6] or luminescent derivative of the labeled molecule when incubated with a proper substrate, allowing it to be detected and quantified.
Horseradish peroxidase has an accessible active site, and many compounds can reach the site of the reaction. On the other hand, for an enzyme such as cytochrome c peroxidase , the compounds that donate electrons are very specific, due to a very narrow active site.
Horseradish peroxidase is also capable of oxidizing these substrates, but its heme is not covalently bound and becomes damaged during turnover. [4] A specific vanadium bromoperoxidase in marine organisms (fungi, bacteria, microalgae, perhaps other eukaryotes) uses vanadate and hydrogen peroxide to brominate electrophilic organics. [5]
Glutathione peroxidase (GPx) (EC 1.11.1.9) is the general name of an enzyme family with peroxidase activity whose main biological role is to protect the organism from oxidative damage. [2] The biochemical function of glutathione peroxidase is to reduce lipid hydroperoxides to their corresponding alcohols and to reduce free hydrogen peroxide to ...
Horseradish peroxidase is commonly linked to secondary antibodies to allow the detection of the target protein by chemiluminescence. The chemiluminescent substrate is cleaved by horseradish peroxidase, resulting in the production of luminescence. Therefore, the production of luminescence is proportional to the amount of horseradish peroxidase ...
Lipid peroxidation is a self-propagating chain reaction and will proceed until the lipid substrate is consumed and the last two remaining radicals combine, or a reaction which terminates it occurs. [3] Termination can occur when two lipid hydroperoxyl radicals (LOO•) react to form peroxide and oxygen (O 2).
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