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Article: Effect of O2, ACC and CO2 concentration on the activity of partially purified ACC oxidase from papaya

TitleEffect of O2, ACC and CO2 concentration on the activity of partially purified ACC oxidase from papaya
O2 、ACC和CO2 對番木瓜ACC氧化酶活性的影響英文)
Authors
KeywordsACC oxidase
Carica papaya L.
CO2
Fe2+
Inhibitor
Issue Date2001
Publisher上海科學技術出版社.
Citation
植物生理学报, 2001, v. 27 n. 5, p. 387-392 How to Cite?
Acta Phytophysiologica Sinica, 2001, v. 27 n. 5, p. 387-392 How to Cite?
AbstractAminocyclopropane 1 carboxlic acid (ACC) is oxidized to form ethylene by ACC oxidase. The partial purification of ACC oxidase from fruit peels of papaya and effects of substrates (oxygen and ACC), cofactors (CO 2 and Fe 2+ ) and inhibitors (Co 2+ and α aminoisobutyric acid) on in vitro ethylene production rate were investigated. ACC oxidase has been purified 19.5 fold by using DEAE Sepharose and Phenyl Sepharose columns. The K m value by ACC oxidase for O 2 in ethylene production varied greatly depending on the ACC concentration, and decreased with increase of ACC levels. The K m value for ACC also declined as oxygen concentration increased. The enzyme activity was dramatically increased by CO 2, and the K m value for O 2 and for ACC increased with increase of CO 2 concentration. Enzyme activities were obviously increased by Fe 2+ and significantly inhibited by Co 2+ ; and Fe 2+ could antagonize the inhibitory role of Co 2+ . These kinetic data are consistent with the view that the catalytic role of ACC oxidase follows an ordered binding mechanism in which ACC oxidase binds first to O 2 and then to ACC.
Persistent Identifierhttp://hdl.handle.net/10722/68438
ISSN

 

DC FieldValueLanguage
dc.contributor.authorSong, SQen_HK
dc.contributor.authorYip, WKen_HK
dc.date.accessioned2010-09-06T06:04:37Z-
dc.date.available2010-09-06T06:04:37Z-
dc.date.issued2001en_HK
dc.identifier.citation植物生理学报, 2001, v. 27 n. 5, p. 387-392en_HK
dc.identifier.citationActa Phytophysiologica Sinica, 2001, v. 27 n. 5, p. 387-392-
dc.identifier.issn0257-4829-
dc.identifier.urihttp://hdl.handle.net/10722/68438-
dc.description.abstractAminocyclopropane 1 carboxlic acid (ACC) is oxidized to form ethylene by ACC oxidase. The partial purification of ACC oxidase from fruit peels of papaya and effects of substrates (oxygen and ACC), cofactors (CO 2 and Fe 2+ ) and inhibitors (Co 2+ and α aminoisobutyric acid) on in vitro ethylene production rate were investigated. ACC oxidase has been purified 19.5 fold by using DEAE Sepharose and Phenyl Sepharose columns. The K m value by ACC oxidase for O 2 in ethylene production varied greatly depending on the ACC concentration, and decreased with increase of ACC levels. The K m value for ACC also declined as oxygen concentration increased. The enzyme activity was dramatically increased by CO 2, and the K m value for O 2 and for ACC increased with increase of CO 2 concentration. Enzyme activities were obviously increased by Fe 2+ and significantly inhibited by Co 2+ ; and Fe 2+ could antagonize the inhibitory role of Co 2+ . These kinetic data are consistent with the view that the catalytic role of ACC oxidase follows an ordered binding mechanism in which ACC oxidase binds first to O 2 and then to ACC.-
dc.languageengen_HK
dc.publisher上海科學技術出版社.-
dc.relation.ispartof植物生理学报en_HK
dc.relation.ispartofActa Phytophysiologica Sinica-
dc.subjectACC oxidase-
dc.subjectCarica papaya L.-
dc.subjectCO2-
dc.subjectFe2+-
dc.subjectInhibitor-
dc.titleEffect of O2, ACC and CO2 concentration on the activity of partially purified ACC oxidase from papayaen_HK
dc.titleO2 、ACC和CO2 對番木瓜ACC氧化酶活性的影響英文)-
dc.typeArticleen_HK
dc.identifier.emailYip, WK: wkyip@hkucc.hku.hken_HK
dc.identifier.authorityYip, WK=rp00833en_HK
dc.identifier.doi10.3321/j.issn:1671-3877.2001.05.005-
dc.identifier.hkuros71755en_HK
dc.identifier.volume27-
dc.identifier.issue5-
dc.identifier.spage387-
dc.identifier.epage392-
dc.publisher.placeChina-

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