Loading…

Hydrogen peroxide is a product of oxygen consumption byTrichomonas vaginalis

The amitochondriate sexually-transmitted human parasitic protozoanTrichomonas vaginalis (Bushby strain) grown anaerobically on complex medium containing cysteine and ascorbic acid consumed O^sub 2^ avidly (6.9 μM min^sup -1^ per 10^sup 6^ organisms) with an apparentK ^sub m^ value of 5.1 μM O^sub 2^...

Full description

Saved in:
Bibliographic Details
Published in:Journal of biosciences 1999-09, Vol.24 (3), p.339-344
Main Authors: Chapman, Alan, Linstead, David J., Lloyd, David
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c1036-f2954c0f629157b866ca09de29ecad59491fa9f0ee6be67326469758512df0113
cites cdi_FETCH-LOGICAL-c1036-f2954c0f629157b866ca09de29ecad59491fa9f0ee6be67326469758512df0113
container_end_page 344
container_issue 3
container_start_page 339
container_title Journal of biosciences
container_volume 24
creator Chapman, Alan
Linstead, David J.
Lloyd, David
description The amitochondriate sexually-transmitted human parasitic protozoanTrichomonas vaginalis (Bushby strain) grown anaerobically on complex medium containing cysteine and ascorbic acid consumed O^sub 2^ avidly (6.9 μM min^sup -1^ per 10^sup 6^ organisms) with an apparentK ^sub m^ value of 5.1 μM O^sub 2^ : O^sub 2^ uptake was inhibited by O^sub 2^ > 120 μM. Spectrophotometric assays in the presence of microperoxidase (419-407 nm) indicated that H^sub 2^O^sub 2^ was produced and that inhibition by high O^sub 2^ concentrations was again evident. Hydrogenosomes oxidizing pyruvate in the presence of ADP and succinate showed similar patterns of O^sub 2^ consumption, H^sub 2^O^sub 2^ production (33.5 pmol min^sup -1^ per mg protein), and O^sub 2^ inhibition. Cytosolic NADH oxidase gave no detectable H^sub 2^O^sub 2^, whereas the cytosolic NADPH oxidase produced H^sub 2^O^sub 2^ at a rate (43 pmol min^sup -1^ per mg protein) greater than that of hydrogenosomes. These results are discussed in relation to the oxidative stress experienced by the pathogen in its natural habitat.[PUBLICATION ABSTRACT]
doi_str_mv 10.1007/BF02941248
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_journals_236236666</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1939949881</sourcerecordid><originalsourceid>FETCH-LOGICAL-c1036-f2954c0f629157b866ca09de29ecad59491fa9f0ee6be67326469758512df0113</originalsourceid><addsrcrecordid>eNpFkFFLwzAUhYMoOKcv_oLgo1C9SZq091GHc8LAl_lcsjSZGVtTk1bWf7-OCV4u3APncPk4hNwzeGIAxfPrHDjmjOflBZkAFiIrmCgvR80lZBKRXZOblLYADHMBE7JcDHUMG9vQ1sZw8LWlPlFN2xjq3nQ0OBoOw8k3oUn9vu18aOh6WEVvvsM-NDrRX73xjd75dEuunN4le_d3p-Rr_raaLbLl5_vH7GWZGQZCZY6jzA04xZHJYl0qZTRgbTlao2uJOTKn0YG1am1VIbjKFRaylIzXDhgTU_Jw_jtS_vQ2ddU29HFESBUXatxxxtDjOWRiSClaV7XR73UcKgbVqazqvyxxBOT9W4M</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>236236666</pqid></control><display><type>article</type><title>Hydrogen peroxide is a product of oxygen consumption byTrichomonas vaginalis</title><source>Springer Nature</source><creator>Chapman, Alan ; Linstead, David J. ; Lloyd, David</creator><creatorcontrib>Chapman, Alan ; Linstead, David J. ; Lloyd, David</creatorcontrib><description>The amitochondriate sexually-transmitted human parasitic protozoanTrichomonas vaginalis (Bushby strain) grown anaerobically on complex medium containing cysteine and ascorbic acid consumed O^sub 2^ avidly (6.9 μM min^sup -1^ per 10^sup 6^ organisms) with an apparentK ^sub m^ value of 5.1 μM O^sub 2^ : O^sub 2^ uptake was inhibited by O^sub 2^ &gt; 120 μM. Spectrophotometric assays in the presence of microperoxidase (419-407 nm) indicated that H^sub 2^O^sub 2^ was produced and that inhibition by high O^sub 2^ concentrations was again evident. Hydrogenosomes oxidizing pyruvate in the presence of ADP and succinate showed similar patterns of O^sub 2^ consumption, H^sub 2^O^sub 2^ production (33.5 pmol min^sup -1^ per mg protein), and O^sub 2^ inhibition. Cytosolic NADH oxidase gave no detectable H^sub 2^O^sub 2^, whereas the cytosolic NADPH oxidase produced H^sub 2^O^sub 2^ at a rate (43 pmol min^sup -1^ per mg protein) greater than that of hydrogenosomes. These results are discussed in relation to the oxidative stress experienced by the pathogen in its natural habitat.[PUBLICATION ABSTRACT]</description><identifier>ISSN: 0250-5991</identifier><identifier>EISSN: 0973-7138</identifier><identifier>DOI: 10.1007/BF02941248</identifier><language>eng</language><publisher>Dordrecht: Springer Nature B.V</publisher><subject>Hydrogen peroxide ; Oxidative stress ; Oxygen ; Oxygen consumption</subject><ispartof>Journal of biosciences, 1999-09, Vol.24 (3), p.339-344</ispartof><rights>Indian Academy of Sciences 1999</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c1036-f2954c0f629157b866ca09de29ecad59491fa9f0ee6be67326469758512df0113</citedby><cites>FETCH-LOGICAL-c1036-f2954c0f629157b866ca09de29ecad59491fa9f0ee6be67326469758512df0113</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27922,27923</link.rule.ids></links><search><creatorcontrib>Chapman, Alan</creatorcontrib><creatorcontrib>Linstead, David J.</creatorcontrib><creatorcontrib>Lloyd, David</creatorcontrib><title>Hydrogen peroxide is a product of oxygen consumption byTrichomonas vaginalis</title><title>Journal of biosciences</title><description>The amitochondriate sexually-transmitted human parasitic protozoanTrichomonas vaginalis (Bushby strain) grown anaerobically on complex medium containing cysteine and ascorbic acid consumed O^sub 2^ avidly (6.9 μM min^sup -1^ per 10^sup 6^ organisms) with an apparentK ^sub m^ value of 5.1 μM O^sub 2^ : O^sub 2^ uptake was inhibited by O^sub 2^ &gt; 120 μM. Spectrophotometric assays in the presence of microperoxidase (419-407 nm) indicated that H^sub 2^O^sub 2^ was produced and that inhibition by high O^sub 2^ concentrations was again evident. Hydrogenosomes oxidizing pyruvate in the presence of ADP and succinate showed similar patterns of O^sub 2^ consumption, H^sub 2^O^sub 2^ production (33.5 pmol min^sup -1^ per mg protein), and O^sub 2^ inhibition. Cytosolic NADH oxidase gave no detectable H^sub 2^O^sub 2^, whereas the cytosolic NADPH oxidase produced H^sub 2^O^sub 2^ at a rate (43 pmol min^sup -1^ per mg protein) greater than that of hydrogenosomes. These results are discussed in relation to the oxidative stress experienced by the pathogen in its natural habitat.[PUBLICATION ABSTRACT]</description><subject>Hydrogen peroxide</subject><subject>Oxidative stress</subject><subject>Oxygen</subject><subject>Oxygen consumption</subject><issn>0250-5991</issn><issn>0973-7138</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNpFkFFLwzAUhYMoOKcv_oLgo1C9SZq091GHc8LAl_lcsjSZGVtTk1bWf7-OCV4u3APncPk4hNwzeGIAxfPrHDjmjOflBZkAFiIrmCgvR80lZBKRXZOblLYADHMBE7JcDHUMG9vQ1sZw8LWlPlFN2xjq3nQ0OBoOw8k3oUn9vu18aOh6WEVvvsM-NDrRX73xjd75dEuunN4le_d3p-Rr_raaLbLl5_vH7GWZGQZCZY6jzA04xZHJYl0qZTRgbTlao2uJOTKn0YG1am1VIbjKFRaylIzXDhgTU_Jw_jtS_vQ2ddU29HFESBUXatxxxtDjOWRiSClaV7XR73UcKgbVqazqvyxxBOT9W4M</recordid><startdate>199909</startdate><enddate>199909</enddate><creator>Chapman, Alan</creator><creator>Linstead, David J.</creator><creator>Lloyd, David</creator><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>F1W</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H99</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L.F</scope><scope>L.G</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope></search><sort><creationdate>199909</creationdate><title>Hydrogen peroxide is a product of oxygen consumption byTrichomonas vaginalis</title><author>Chapman, Alan ; Linstead, David J. ; Lloyd, David</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c1036-f2954c0f629157b866ca09de29ecad59491fa9f0ee6be67326469758512df0113</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Hydrogen peroxide</topic><topic>Oxidative stress</topic><topic>Oxygen</topic><topic>Oxygen consumption</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chapman, Alan</creatorcontrib><creatorcontrib>Linstead, David J.</creatorcontrib><creatorcontrib>Lloyd, David</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Nucleic Acids Abstracts</collection><collection>Health &amp; Medical Collection (ProQuest Medical &amp; Health Databases)</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ASFA: Marine Biotechnology Abstracts</collection><collection>SciTech Premium Collection (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Aquatic Science &amp; Fisheries Abstracts (ASFA) Marine Biotechnology Abstracts</collection><collection>Aquatic Science &amp; Fisheries Abstracts (ASFA) Professional</collection><collection>ProQuest Biological Science Collection</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest research library</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><jtitle>Journal of biosciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chapman, Alan</au><au>Linstead, David J.</au><au>Lloyd, David</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hydrogen peroxide is a product of oxygen consumption byTrichomonas vaginalis</atitle><jtitle>Journal of biosciences</jtitle><date>1999-09</date><risdate>1999</risdate><volume>24</volume><issue>3</issue><spage>339</spage><epage>344</epage><pages>339-344</pages><issn>0250-5991</issn><eissn>0973-7138</eissn><abstract>The amitochondriate sexually-transmitted human parasitic protozoanTrichomonas vaginalis (Bushby strain) grown anaerobically on complex medium containing cysteine and ascorbic acid consumed O^sub 2^ avidly (6.9 μM min^sup -1^ per 10^sup 6^ organisms) with an apparentK ^sub m^ value of 5.1 μM O^sub 2^ : O^sub 2^ uptake was inhibited by O^sub 2^ &gt; 120 μM. Spectrophotometric assays in the presence of microperoxidase (419-407 nm) indicated that H^sub 2^O^sub 2^ was produced and that inhibition by high O^sub 2^ concentrations was again evident. Hydrogenosomes oxidizing pyruvate in the presence of ADP and succinate showed similar patterns of O^sub 2^ consumption, H^sub 2^O^sub 2^ production (33.5 pmol min^sup -1^ per mg protein), and O^sub 2^ inhibition. Cytosolic NADH oxidase gave no detectable H^sub 2^O^sub 2^, whereas the cytosolic NADPH oxidase produced H^sub 2^O^sub 2^ at a rate (43 pmol min^sup -1^ per mg protein) greater than that of hydrogenosomes. These results are discussed in relation to the oxidative stress experienced by the pathogen in its natural habitat.[PUBLICATION ABSTRACT]</abstract><cop>Dordrecht</cop><pub>Springer Nature B.V</pub><doi>10.1007/BF02941248</doi><tpages>6</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0250-5991
ispartof Journal of biosciences, 1999-09, Vol.24 (3), p.339-344
issn 0250-5991
0973-7138
language eng
recordid cdi_proquest_journals_236236666
source Springer Nature
subjects Hydrogen peroxide
Oxidative stress
Oxygen
Oxygen consumption
title Hydrogen peroxide is a product of oxygen consumption byTrichomonas vaginalis
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-14T00%3A40%3A27IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Hydrogen%20peroxide%20is%20a%20product%20of%20oxygen%20consumption%20byTrichomonas%20vaginalis&rft.jtitle=Journal%20of%20biosciences&rft.au=Chapman,%20Alan&rft.date=1999-09&rft.volume=24&rft.issue=3&rft.spage=339&rft.epage=344&rft.pages=339-344&rft.issn=0250-5991&rft.eissn=0973-7138&rft_id=info:doi/10.1007/BF02941248&rft_dat=%3Cproquest_cross%3E1939949881%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c1036-f2954c0f629157b866ca09de29ecad59491fa9f0ee6be67326469758512df0113%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=236236666&rft_id=info:pmid/&rfr_iscdi=true