<?xml version="1.0"?>
<Articles JournalTitle="Iranian Journal of Public Health">
  <Article>
    <Journal>
      <PublisherName>Tehran University of Medical Sciences</PublisherName>
      <JournalTitle>Iranian Journal of Public Health</JournalTitle>
      <Issn>2251-6085</Issn>
      <Volume>35</Volume>
      <Issue>2</Issue>
      <PubDate PubStatus="epublish">
        <Year>2006</Year>
        <Month>06</Month>
        <Day>15</Day>
      </PubDate>
    </Journal>
    <title locale="en_US">Effect of Mercuric Chloride on Kinetic Properties of Horseradish Peroxidase</title>
    <FirstPage>49</FirstPage>
    <LastPage>56</LastPage>
    <AuthorList>
      <Author>
        <FirstName></FirstName>
        <LastName>N Einollahi</LastName>
        <affiliation locale="en_US"></affiliation>
      </Author>
      <Author>
        <FirstName></FirstName>
        <LastName>S Abbasi</LastName>
        <affiliation locale="en_US"></affiliation>
      </Author>
      <Author>
        <FirstName></FirstName>
        <LastName>N Dashti</LastName>
        <affiliation locale="en_US"></affiliation>
      </Author>
      <Author>
        <FirstName></FirstName>
        <LastName>F Vaezzadeh</LastName>
        <affiliation locale="en_US"></affiliation>
      </Author>
    </AuthorList>
    <History>
      <PubDate PubStatus="received">
        <Year>2015</Year>
        <Month>10</Month>
        <Day>03</Day>
      </PubDate>
    </History>
    <abstract locale="en_US">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 &#xF06D;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.</abstract>
    <web_url>https://ijph.tums.ac.ir/index.php/ijph/article/view/2179</web_url>
    <pdf_url>https://ijph.tums.ac.ir/index.php/ijph/article/download/2179/2160</pdf_url>
  </Article>
</Articles>
