Effect of Mercuric Chloride on Kinetic Properties of Horseradish Peroxidase
Mercury is one of the three major environmental metal poisons, and mercuric chloride is a highly reactive compound which can harm cells by a variety of mechanisms including direct interaction with sulphydryl groups of proteins and enzymes, therefore affecting the enzymatic activity. This study focus...
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Tehran University of Medical Sciences
2006-06-01
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Online Access: | https://ijph.tums.ac.ir/index.php/ijph/article/view/2179 |
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doaj-de47a33ad76b44f1b7e282fbed63949c2020-12-02T18:51:59ZengTehran University of Medical SciencesIranian Journal of Public Health2251-60852251-60932006-06-01352Effect of Mercuric Chloride on Kinetic Properties of Horseradish Peroxidase N Einollahi0 S Abbasi1 N Dashti2 F Vaezzadeh3 Mercury is one of the three major environmental metal poisons, and mercuric chloride is a highly reactive compound which can harm cells by a variety of mechanisms including direct interaction with sulphydryl groups of proteins and enzymes, therefore affecting the enzymatic activity. This study focused on the effect of Hg++ on horseradish peroxidase (donor: hydrogen peroxide oxidoreductase, EC 1.11.1.7) (HRP) (Isoenzyme C) activity. In the presence of 88 mM hydrogen peroxide Km for o-dianisidine oxidation was 0.05 millimolar and Vmax was 8.5 M.s-1. Incubation of the enzyme with 1 to 100 millimolar mercuric chloride for 5-20- and 60 min resulted in progressive inhibition of the enzymatic activity. At low Hg++ concentrations the inhibition was reversible by excess substrate, while at high Hg++ concentration the inhibition was not reversible. Results also indicated that the type of inhibition depended on the duration of incubation of the enzyme with metal ion and on the Hg++ concentration. So we could conclude that the type of inhibition changed from noncompetitive to mix with increased incubation time and increased metal concentration. https://ijph.tums.ac.ir/index.php/ijph/article/view/2179Horseradish peroxidaseMercuric chlorideEnzyme inhibitionO dianisidine |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
N Einollahi S Abbasi N Dashti F Vaezzadeh |
spellingShingle |
N Einollahi S Abbasi N Dashti F Vaezzadeh Effect of Mercuric Chloride on Kinetic Properties of Horseradish Peroxidase Iranian Journal of Public Health Horseradish peroxidase Mercuric chloride Enzyme inhibition O dianisidine |
author_facet |
N Einollahi S Abbasi N Dashti F Vaezzadeh |
author_sort |
N Einollahi |
title |
Effect of Mercuric Chloride on Kinetic Properties of Horseradish Peroxidase |
title_short |
Effect of Mercuric Chloride on Kinetic Properties of Horseradish Peroxidase |
title_full |
Effect of Mercuric Chloride on Kinetic Properties of Horseradish Peroxidase |
title_fullStr |
Effect of Mercuric Chloride on Kinetic Properties of Horseradish Peroxidase |
title_full_unstemmed |
Effect of Mercuric Chloride on Kinetic Properties of Horseradish Peroxidase |
title_sort |
effect of mercuric chloride on kinetic properties of horseradish peroxidase |
publisher |
Tehran University of Medical Sciences |
series |
Iranian Journal of Public Health |
issn |
2251-6085 2251-6093 |
publishDate |
2006-06-01 |
description |
Mercury is one of the three major environmental metal poisons, and mercuric chloride is a highly reactive compound which can harm cells by a variety of mechanisms including direct interaction with sulphydryl groups of proteins and enzymes, therefore affecting the enzymatic activity. This study focused on the effect of Hg++ on horseradish peroxidase (donor: hydrogen peroxide oxidoreductase, EC 1.11.1.7) (HRP) (Isoenzyme C) activity. In the presence of 88 mM hydrogen peroxide Km for o-dianisidine oxidation was 0.05 millimolar and Vmax was 8.5 M.s-1. Incubation of the enzyme with 1 to 100 millimolar mercuric chloride for 5-20- and 60 min resulted in progressive inhibition of the enzymatic activity. At low Hg++ concentrations the inhibition was reversible by excess substrate, while at high Hg++ concentration the inhibition was not reversible. Results also indicated that the type of inhibition depended on the duration of incubation of the enzyme with metal ion and on the Hg++ concentration. So we could conclude that the type of inhibition changed from noncompetitive to mix with increased incubation time and increased metal concentration. |
topic |
Horseradish peroxidase Mercuric chloride Enzyme inhibition O dianisidine |
url |
https://ijph.tums.ac.ir/index.php/ijph/article/view/2179 |
work_keys_str_mv |
AT neinollahi effectofmercuricchlorideonkineticpropertiesofhorseradishperoxidase AT sabbasi effectofmercuricchlorideonkineticpropertiesofhorseradishperoxidase AT ndashti effectofmercuricchlorideonkineticpropertiesofhorseradishperoxidase AT fvaezzadeh effectofmercuricchlorideonkineticpropertiesofhorseradishperoxidase |
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1724402910734843904 |