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Article: Immunopurification and characterization of a 40-kD 1-aminocyclopropane-1-carboxylic acid N-malonyltransferase from mung bean seedling hypocotyls

TitleImmunopurification and characterization of a 40-kD 1-aminocyclopropane-1-carboxylic acid N-malonyltransferase from mung bean seedling hypocotyls
Authors
Issue Date1997
PublisherAmerican Society of Plant Biologists. The Journal's web site is located at http://www.plantphysiol.org
Citation
Plant Physiology, 1997, v. 113 n. 1, p. 119-126 How to Cite?
Abstract1-Aminocyclopropane-1-carboxylic acid (ACC) N-malonyltransferase catalyzes the transfer of the malonyl group from malonyl coenzyme A to ACC to form malonyl ACC. Using partially purified ACC N-malonyltransferase from the hypocotyls of mung bean (Vigna radiata) seedlings, we produced two mouse monoclonal antibodies (1H5 and 2G3) to this enzyme. These antibodies bind to sites other than the active site of the enzyme because monoclonal antibody-bound ACC N-malonyltransferase still exhibits full catalytic activity. A monoclonal antibody column was constructed using 1H5 and protein G Sepharose. The ACC N-malonyltransferase purified from this monoclonal antibody column has a molecular mass of 40 kD, which is different from that reported previously. The enzyme has a higher electrophoretic mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the absence of the reducing agent dithiothreitol. The optimum temperature of this 40-kD ACC N-malonyltransferase is 45 degrees C and the apparent Kms for ACC and malonyl coenzyme A are 66.7 and 40 microns, respectively.
Persistent Identifierhttp://hdl.handle.net/10722/49352
ISSN
2015 Impact Factor: 6.28
2015 SCImago Journal Rankings: 3.642
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorChick, WSHen_HK
dc.contributor.authorLeung, PCen_HK
dc.date.accessioned2008-06-12T06:40:09Z-
dc.date.available2008-06-12T06:40:09Z-
dc.date.issued1997en_HK
dc.identifier.citationPlant Physiology, 1997, v. 113 n. 1, p. 119-126en_HK
dc.identifier.issn0032-0889en_HK
dc.identifier.urihttp://hdl.handle.net/10722/49352-
dc.description.abstract1-Aminocyclopropane-1-carboxylic acid (ACC) N-malonyltransferase catalyzes the transfer of the malonyl group from malonyl coenzyme A to ACC to form malonyl ACC. Using partially purified ACC N-malonyltransferase from the hypocotyls of mung bean (Vigna radiata) seedlings, we produced two mouse monoclonal antibodies (1H5 and 2G3) to this enzyme. These antibodies bind to sites other than the active site of the enzyme because monoclonal antibody-bound ACC N-malonyltransferase still exhibits full catalytic activity. A monoclonal antibody column was constructed using 1H5 and protein G Sepharose. The ACC N-malonyltransferase purified from this monoclonal antibody column has a molecular mass of 40 kD, which is different from that reported previously. The enzyme has a higher electrophoretic mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the absence of the reducing agent dithiothreitol. The optimum temperature of this 40-kD ACC N-malonyltransferase is 45 degrees C and the apparent Kms for ACC and malonyl coenzyme A are 66.7 and 40 microns, respectively.en_HK
dc.format.extent418 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
dc.publisherAmerican Society of Plant Biologists. The Journal's web site is located at http://www.plantphysiol.orgen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subject.meshAcyltransferases - isolation & purification - metabolismen_HK
dc.subject.meshFabaceae - enzymologyen_HK
dc.subject.meshPlants, Medicinalen_HK
dc.subject.meshChromatography, Affinityen_HK
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_HK
dc.titleImmunopurification and characterization of a 40-kD 1-aminocyclopropane-1-carboxylic acid N-malonyltransferase from mung bean seedling hypocotylsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0032-0889&volume=113&issue=1&spage=119&epage=126&date=1997&atitle=Immunopurification+and+characterization+of+a+40-kD+1-aminocyclopropane-1-carboxylic+acid+N-malonyltransferase+from+mung+bean+seedling+hypocotylsen_HK
dc.identifier.emailLeung, PC: pcleung@hkucc.hku.hken_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.pmid9008392-
dc.identifier.pmcidPMC158122-
dc.identifier.scopuseid_2-s2.0-1842411894-
dc.identifier.hkuros22492-
dc.identifier.isiWOS:A1997WC70600015-

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