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Article: Purification of 5-aminolaevulinate synthase from liver mitochondria of chick embryo.

TitlePurification of 5-aminolaevulinate synthase from liver mitochondria of chick embryo.
Authors
Issue Date1983
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EJB
Citation
European Journal Of Biochemistry, 1983, v. 129 n. 3, p. 615-620 How to Cite?
Abstract5-Aminolaevulinate synthase from chick-embryo liver mitochondria has, for the first time, been purified to homogeneity in its native non-degraded form by molecular sieve chromatography, chromatofocusing and affinity chromatography. The enzyme has a minimum molecular weight of 68000 as determined by sodium dodecylsulphate/polyacrylamide gel electrophoresis and a specific activity of 35000 units/mg of protein. This result conflicts with the previous report of Whiting, M.J. and Granick, G. [(1976) J. Biol. Chem. 251, 1340-1346] that the chick embryo enzyme has a molecular weight of 49000. We show here that the purified form can be degraded proteolytically to a smaller form of molecular weight around 50000 while retaining full enzymatic activity. It seem evident, therefore, that the enzyme isolated by Whiting & Granick (1976) was degraded. We have further established by pulse-labelling studies and immunoprecipitation that the enzyme isolated by our new and rapid procedure has the same minimum molecular weight as that which exists in vivo.
Persistent Identifierhttp://hdl.handle.net/10722/147734
ISSN
2006 Impact Factor: 3.579
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorBorthwick, IAen_US
dc.contributor.authorSrivastava, Gen_US
dc.contributor.authorBrooker, JDen_US
dc.contributor.authorMay, BKen_US
dc.contributor.authorElliott, WHen_US
dc.date.accessioned2012-05-29T06:08:58Z-
dc.date.available2012-05-29T06:08:58Z-
dc.date.issued1983en_US
dc.identifier.citationEuropean Journal Of Biochemistry, 1983, v. 129 n. 3, p. 615-620en_US
dc.identifier.issn0014-2956en_US
dc.identifier.urihttp://hdl.handle.net/10722/147734-
dc.description.abstract5-Aminolaevulinate synthase from chick-embryo liver mitochondria has, for the first time, been purified to homogeneity in its native non-degraded form by molecular sieve chromatography, chromatofocusing and affinity chromatography. The enzyme has a minimum molecular weight of 68000 as determined by sodium dodecylsulphate/polyacrylamide gel electrophoresis and a specific activity of 35000 units/mg of protein. This result conflicts with the previous report of Whiting, M.J. and Granick, G. [(1976) J. Biol. Chem. 251, 1340-1346] that the chick embryo enzyme has a molecular weight of 49000. We show here that the purified form can be degraded proteolytically to a smaller form of molecular weight around 50000 while retaining full enzymatic activity. It seem evident, therefore, that the enzyme isolated by Whiting & Granick (1976) was degraded. We have further established by pulse-labelling studies and immunoprecipitation that the enzyme isolated by our new and rapid procedure has the same minimum molecular weight as that which exists in vivo.en_US
dc.languageengen_US
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EJBen_US
dc.relation.ispartofEuropean Journal of Biochemistryen_US
dc.subject.mesh5-Aminolevulinate Synthetase - Isolation & Purificationen_US
dc.subject.meshAnimalsen_US
dc.subject.meshChick Embryoen_US
dc.subject.meshChromatography - Methodsen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshMitochondria, Liver - Enzymologyen_US
dc.subject.meshMolecular Weighten_US
dc.titlePurification of 5-aminolaevulinate synthase from liver mitochondria of chick embryo.en_US
dc.typeArticleen_US
dc.identifier.emailSrivastava, G:gopesh@pathology.hku.hken_US
dc.identifier.authoritySrivastava, G=rp00365en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid6825676en_US
dc.identifier.scopuseid_2-s2.0-0020696101en_US
dc.identifier.volume129en_US
dc.identifier.issue3en_US
dc.identifier.spage615en_US
dc.identifier.epage620en_US
dc.identifier.isiWOS:A1983PY02200017-
dc.publisher.placeUnited Kingdomen_US

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