ATPase membranaire de vacuoles lysosomales: Les lutoides du latex d' Hevea brasiliensis
Identifieur interne : 000175 ( France/Analysis ); précédent : 000174; suivant : 000176ATPase membranaire de vacuoles lysosomales: Les lutoides du latex d' Hevea brasiliensis
Auteurs : Jean D'Auzac [France]Source :
- Phytochemistry [ 0031-9422 ] ; 1977.
Abstract
Membranes of the lutoids present in the latex of Hevea brasiliensis possess an ATPase which is separable from adsorbed residual acid phosphatase. The pH optimum of the ATPase is 7.75 in Tris—HCl and is displaced to 6.5 in K-phosphate buffer. A divalent cation is obligatory (Mg Mn > Ca). ATP-Mg is the natural substrate of the enzyme. Monovalent cations have practically no action on the enzyme. It is, however, activated by anions, both inorganic (Cl−, HCO3−) and organic (malate, aspartate, tartrate). The enzyme has a higher specificity for ATP than for GTP, CTP or UTP and is non-competitively inhibited by ADP. The enzyme is temperature sensitive and a break in the Arrhenius plot occurs at about 20°, characteristic of membrane-bound enzymes. SH-group poisons inhibit enzyme activity as do classical uncouplers at high concentrations (about 10−3 M). A hypothesis is formulated whereby the membrane-bound lutoid ATPase functions as a proton pump in order to maintain the acid pH of a vacuolar and lysosomal compartment.
Url:
DOI: 10.1016/0031-9422(77)80088-5
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 001563
- to stream Istex, to step Curation: 001563
- to stream Istex, to step Checkpoint: 001936
- to stream Main, to step Merge: 001F89
- to stream Main, to step Curation: 001E72
- to stream Main, to step Exploration: 001E72
- to stream France, to step Extraction: 000175
Links to Exploration step
ISTEX:7F9B81B08A37D240069D1A1316C688201E62EEFBLe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="fr">ATPase membranaire de vacuoles lysosomales: Les lutoides du latex d' Hevea brasiliensis</title><author><name sortKey="D Auzac, Jean" sort="D Auzac, Jean" uniqKey="D Auzac J" first="Jean" last="D'Auzac">Jean D'Auzac</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:7F9B81B08A37D240069D1A1316C688201E62EEFB</idno><date when="1977" year="1977">1977</date><idno type="doi">10.1016/0031-9422(77)80088-5</idno><idno type="url">https://api.istex.fr/document/7F9B81B08A37D240069D1A1316C688201E62EEFB/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">001563</idno><idno type="wicri:Area/Istex/Curation">001563</idno><idno type="wicri:Area/Istex/Checkpoint">001936</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">001936</idno><idno type="wicri:doubleKey">0031-9422:1977:D Auzac J:atpase:membranaire:de</idno><idno type="wicri:Area/Main/Merge">001F89</idno><idno type="wicri:Area/Main/Curation">001E72</idno><idno type="wicri:Area/Main/Exploration">001E72</idno><idno type="wicri:Area/France/Extraction">000175</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="fr">ATPase membranaire de vacuoles lysosomales: Les lutoides du latex d' Hevea brasiliensis</title><author><name sortKey="D Auzac, Jean" sort="D Auzac, Jean" uniqKey="D Auzac J" first="Jean" last="D'Auzac">Jean D'Auzac</name><affiliation wicri:level="4"><country xml:lang="fr">France</country><wicri:regionArea>Laboratoire de Physiologie Végétale, Université des Sciences et Techniques du Languedoc, 34060 Montpellier-Cedex</wicri:regionArea><placeName><region type="region" nuts="2">Occitanie (région administrative)</region><region type="old region" nuts="2">Languedoc-Roussillon</region><settlement type="city">Montpellier</settlement></placeName><orgName type="university">Université Montpellier 2</orgName></affiliation></author></analytic><monogr></monogr><series><title level="j">Phytochemistry</title><title level="j" type="abbrev">PHYTO</title><idno type="ISSN">0031-9422</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1977">1977</date><biblScope unit="volume">16</biblScope><biblScope unit="issue">12</biblScope><biblScope unit="page" from="1881">1881</biblScope><biblScope unit="page" to="1885">1885</biblScope></imprint><idno type="ISSN">0031-9422</idno></series><idno type="istex">7F9B81B08A37D240069D1A1316C688201E62EEFB</idno><idno type="DOI">10.1016/0031-9422(77)80088-5</idno><idno type="PII">0031-9422(77)80088-5</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0031-9422</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass><langUsage><language ident="fr">fr</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Membranes of the lutoids present in the latex of Hevea brasiliensis possess an ATPase which is separable from adsorbed residual acid phosphatase. The pH optimum of the ATPase is 7.75 in Tris—HCl and is displaced to 6.5 in K-phosphate buffer. A divalent cation is obligatory (Mg Mn > Ca). ATP-Mg is the natural substrate of the enzyme. Monovalent cations have practically no action on the enzyme. It is, however, activated by anions, both inorganic (Cl−, HCO3−) and organic (malate, aspartate, tartrate). The enzyme has a higher specificity for ATP than for GTP, CTP or UTP and is non-competitively inhibited by ADP. The enzyme is temperature sensitive and a break in the Arrhenius plot occurs at about 20°, characteristic of membrane-bound enzymes. SH-group poisons inhibit enzyme activity as do classical uncouplers at high concentrations (about 10−3 M). A hypothesis is formulated whereby the membrane-bound lutoid ATPase functions as a proton pump in order to maintain the acid pH of a vacuolar and lysosomal compartment.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Languedoc-Roussillon</li><li>Occitanie (région administrative)</li></region><settlement><li>Montpellier</li></settlement><orgName><li>Université Montpellier 2</li></orgName></list><tree><country name="France"><region name="Occitanie (région administrative)"><name sortKey="D Auzac, Jean" sort="D Auzac, Jean" uniqKey="D Auzac J" first="Jean" last="D'Auzac">Jean D'Auzac</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Eau/explor/LotaV3/Data/France/Analysis
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000175 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/France/Analysis/biblio.hfd -nk 000175 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Eau
|area= LotaV3
|flux= France
|étape= Analysis
|type= RBID
|clé= ISTEX:7F9B81B08A37D240069D1A1316C688201E62EEFB
|texte= ATPase membranaire de vacuoles lysosomales: Les lutoides du latex d' Hevea brasiliensis
}}
| This area was generated with Dilib version V0.6.39. |  |