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Article: Purification and characterization of 1-aminocyclopropane-1-carboxylate synthase from apple fruits

TitlePurification and characterization of 1-aminocyclopropane-1-carboxylate synthase from apple fruits
Authors
Issue Date1991
PublisherAmerican Society of Plant Biologists. The Journal's web site is located at http://www.plantphysiol.org
Citation
Plant Physiology, 1991, v. 95 n. 1, p. 251-257 How to Cite?
Abstract1-Aminocyclopropane-1-carboxylate (ACC) synthase, a key enzyme in ethylene biosynthesis, was isolated and partially purified from apple (Malus sylvestris Mill.) fruits. Unlike ACC synthase isolated from other sources, apple ACC synthase is associated with the pellet fraction and can be solubilized in active form with Triton X-100. Following five purification steps, the solubilized enzyme was purified over 5000-fold to a specific activity of 100 micromoles per milligram protein per hour, and its purity was estimated to be 20 to 30%. Using this preparation, specific monoclonal antibodies were raised. Monoclonal antibodies against ACC synthase immunoglobulin were coupled to protein-A agarose to make an immunoaffinity column, which effectively purified the enzyme from a relatively crude enzyme preparation (100 units per milligram protein). As with the tomato enzyme, apple ACC synthase was inactivated and radiolabeled by its substrate S-adenosyl-L-methionine. Apple ACC synthase was identified to be a 48-kilodalton protein based on the observation that it was specifically bound to immunoaffinity column and it was specifically radiolabeled by its substrate S-adenosyl-L-methionine.
Persistent Identifierhttp://hdl.handle.net/10722/178373
ISSN
2015 Impact Factor: 6.28
2015 SCImago Journal Rankings: 3.642

 

DC FieldValueLanguage
dc.contributor.authorYip, WKen_US
dc.contributor.authorDong, JGen_US
dc.contributor.authorYang, SFen_US
dc.date.accessioned2012-12-19T09:47:19Z-
dc.date.available2012-12-19T09:47:19Z-
dc.date.issued1991en_US
dc.identifier.citationPlant Physiology, 1991, v. 95 n. 1, p. 251-257en_US
dc.identifier.issn0032-0889en_US
dc.identifier.urihttp://hdl.handle.net/10722/178373-
dc.description.abstract1-Aminocyclopropane-1-carboxylate (ACC) synthase, a key enzyme in ethylene biosynthesis, was isolated and partially purified from apple (Malus sylvestris Mill.) fruits. Unlike ACC synthase isolated from other sources, apple ACC synthase is associated with the pellet fraction and can be solubilized in active form with Triton X-100. Following five purification steps, the solubilized enzyme was purified over 5000-fold to a specific activity of 100 micromoles per milligram protein per hour, and its purity was estimated to be 20 to 30%. Using this preparation, specific monoclonal antibodies were raised. Monoclonal antibodies against ACC synthase immunoglobulin were coupled to protein-A agarose to make an immunoaffinity column, which effectively purified the enzyme from a relatively crude enzyme preparation (100 units per milligram protein). As with the tomato enzyme, apple ACC synthase was inactivated and radiolabeled by its substrate S-adenosyl-L-methionine. Apple ACC synthase was identified to be a 48-kilodalton protein based on the observation that it was specifically bound to immunoaffinity column and it was specifically radiolabeled by its substrate S-adenosyl-L-methionine.en_US
dc.languageengen_US
dc.publisherAmerican Society of Plant Biologists. The Journal's web site is located at http://www.plantphysiol.orgen_US
dc.relation.ispartofPlant Physiologyen_US
dc.titlePurification and characterization of 1-aminocyclopropane-1-carboxylate synthase from apple fruitsen_US
dc.typeArticleen_US
dc.identifier.emailYip, WK: wkyip@hkucc.hku.hken_US
dc.identifier.authorityYip, WK=rp00833en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.scopuseid_2-s2.0-0001068389en_US
dc.identifier.volume95en_US
dc.identifier.issue1en_US
dc.identifier.spage251en_US
dc.identifier.epage257en_US
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridYip, WK=7102784428en_US
dc.identifier.scopusauthoridDong, JG=55477984500en_US
dc.identifier.scopusauthoridYang, SF=7406946528en_US

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