Glutamine synthetase of pea leaves. I. Purification, stabilization, and pH optima
Identifieur interne : 002C56 ( Main/Exploration ); précédent : 002C55; suivant : 002C57Glutamine synthetase of pea leaves. I. Purification, stabilization, and pH optima
Auteurs : D. O'Neal [Canada] ; K. W. Joy [Canada]Source :
- Archives of Biochemistry and Biophysics [ 0003-9861 ] ; 1973.
English descriptors
- Teeft :
- Academic press, Acetic acid, Assay, Biochem, Calcium phosphate, Carrot, Carrot enzyme, Cation, Chem, Coli enzyme, Divalent, Divalent cation, Enzyme, Ethylene, Ethylene glycol, Final activity, Final concentration, Glutamine, Glutamine synthetase, Glycol, Initial activity, Leaf enzyme, Mgso, Molar ratio, Molecular weight, Norit, Optimal stability, Protamine sulfate, Protein concentration, Protein pellet, Pyruvate kinase, Seed enzyme, Several days, Several weeks, Specific activity, Sucrose, Synthetase.
Abstract
Abstract: 1. Glutamine synthetase [l-glutamate: ammonia ligase (ADP), E.C. 6.3.1.2]was purified to apparent homogeneity from the shoots of light-grown pea seedlings. It was found to be quite unstable, but. could be partially stabilized by the addition of divalent cation (Mg2+ or Mn2+), and still further by the addition of sucrose (0.5–1.5 m), fructose (1–2.5 m), or ethyleneglycol (20–30%). Stability varied considerably depending on pH and whether Mg2+ or Mn2+ was used. Under certain incubation conditions the inactivated enzyme could be partially reactivated. 2. The pH optimum for glutamine synthesis varied widely (5.0–8.2) depending on the type and concentration of divalent cation (Mn2+, Co2+, Mg2+) and the ATP concentration.
Url:
DOI: 10.1016/0003-9861(73)90435-9
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 001299
- to stream Istex, to step Curation: 001299
- to stream Istex, to step Checkpoint: 001801
- to stream Main, to step Merge: 002E31
- to stream Main, to step Curation: 002C56
Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Glutamine synthetase of pea leaves. I. Purification, stabilization, and pH optima</title><author><name sortKey="O Neal, D" sort="O Neal, D" uniqKey="O Neal D" first="D." last="O'Neal">D. O'Neal</name></author><author><name sortKey="Joy, K W" sort="Joy, K W" uniqKey="Joy K" first="K. W." last="Joy">K. W. Joy</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:0E5F40722556E92A529E905D0B3C11B162785E8B</idno><date when="1973" year="1973">1973</date><idno type="doi">10.1016/0003-9861(73)90435-9</idno><idno type="url">https://api.istex.fr/ark:/67375/6H6-4ZQB3VBQ-4/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">001299</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001299</idno><idno type="wicri:Area/Istex/Curation">001299</idno><idno type="wicri:Area/Istex/Checkpoint">001801</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">001801</idno><idno type="wicri:doubleKey">0003-9861:1973:O Neal D:glutamine:synthetase:of</idno><idno type="wicri:Area/Main/Merge">002E31</idno><idno type="wicri:Area/Main/Curation">002C56</idno><idno type="wicri:Area/Main/Exploration">002C56</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Glutamine synthetase of pea leaves. I. Purification, stabilization, and pH optima</title><author><name sortKey="O Neal, D" sort="O Neal, D" uniqKey="O Neal D" first="D." last="O'Neal">D. O'Neal</name><affiliation wicri:level="1"><country xml:lang="fr">Canada</country><wicri:regionArea>Biology Department, Carleton University, Ottawa</wicri:regionArea><wicri:noRegion>Ottawa</wicri:noRegion></affiliation></author><author><name sortKey="Joy, K W" sort="Joy, K W" uniqKey="Joy K" first="K. W." last="Joy">K. W. Joy</name><affiliation wicri:level="1"><country xml:lang="fr">Canada</country><wicri:regionArea>Biology Department, Carleton University, Ottawa</wicri:regionArea><wicri:noRegion>Ottawa</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Archives of Biochemistry and Biophysics</title><title level="j" type="abbrev">YABBI</title><idno type="ISSN">0003-9861</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1973">1973</date><biblScope unit="volume">159</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="113">113</biblScope><biblScope unit="page" to="122">122</biblScope></imprint><idno type="ISSN">0003-9861</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0003-9861</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Academic press</term><term>Acetic acid</term><term>Assay</term><term>Biochem</term><term>Calcium phosphate</term><term>Carrot</term><term>Carrot enzyme</term><term>Cation</term><term>Chem</term><term>Coli enzyme</term><term>Divalent</term><term>Divalent cation</term><term>Enzyme</term><term>Ethylene</term><term>Ethylene glycol</term><term>Final activity</term><term>Final concentration</term><term>Glutamine</term><term>Glutamine synthetase</term><term>Glycol</term><term>Initial activity</term><term>Leaf enzyme</term><term>Mgso</term><term>Molar ratio</term><term>Molecular weight</term><term>Norit</term><term>Optimal stability</term><term>Protamine sulfate</term><term>Protein concentration</term><term>Protein pellet</term><term>Pyruvate kinase</term><term>Seed enzyme</term><term>Several days</term><term>Several weeks</term><term>Specific activity</term><term>Sucrose</term><term>Synthetase</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: 1. Glutamine synthetase [l-glutamate: ammonia ligase (ADP), E.C. 6.3.1.2]was purified to apparent homogeneity from the shoots of light-grown pea seedlings. It was found to be quite unstable, but. could be partially stabilized by the addition of divalent cation (Mg2+ or Mn2+), and still further by the addition of sucrose (0.5–1.5 m), fructose (1–2.5 m), or ethyleneglycol (20–30%). Stability varied considerably depending on pH and whether Mg2+ or Mn2+ was used. Under certain incubation conditions the inactivated enzyme could be partially reactivated. 2. The pH optimum for glutamine synthesis varied widely (5.0–8.2) depending on the type and concentration of divalent cation (Mn2+, Co2+, Mg2+) and the ATP concentration.</div></front></TEI><affiliations><list><country><li>Canada</li></country></list><tree><country name="Canada"><noRegion><name sortKey="O Neal, D" sort="O Neal, D" uniqKey="O Neal D" first="D." last="O'Neal">D. O'Neal</name></noRegion><name sortKey="Joy, K W" sort="Joy, K W" uniqKey="Joy K" first="K. W." last="Joy">K. W. Joy</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/H2N2V1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002C56 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 002C56 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= H2N2V1
|flux= Main
|étape= Exploration
|type= RBID
|clé= ISTEX:0E5F40722556E92A529E905D0B3C11B162785E8B
|texte= Glutamine synthetase of pea leaves. I. Purification, stabilization, and pH optima
}}
| This area was generated with Dilib version V0.6.33. |  |