File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Purification of rat liver mitochondrial δ-aminolaevulinate synthase

TitlePurification of rat liver mitochondrial δ-aminolaevulinate synthase
Authors
Issue Date1982
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description
Citation
Biochemical And Biophysical Research Communications, 1982, v. 109 n. 2, p. 305-312 How to Cite?
AbstractMitochondrial δ-aminolaevulinate synthase was purified from drug-induced adult rat liver and identified for the first time as a protein of minimum molecular weight 70,000. The enzyme was also identified in mitochondria by pulse-labelling and immunoprecipitation and shown to have a molecular weight of 70,000. The purified enzyme was degraded by papain to smaller forms of molecular weight about 56,000 with no loss of enzyme activity. In vitro translation experiments suggest that the enzyme is synthesized initially as a larger precursor of molecular weight 76,000. © 1982.
Persistent Identifierhttp://hdl.handle.net/10722/147731
ISSN
2015 Impact Factor: 2.371
2015 SCImago Journal Rankings: 1.152
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorSrivastava, Gen_US
dc.contributor.authorBorthwick, IAen_US
dc.contributor.authorBrooker, JDen_US
dc.contributor.authorMay, BKen_US
dc.contributor.authorElliott, WHen_US
dc.date.accessioned2012-05-29T06:08:57Z-
dc.date.available2012-05-29T06:08:57Z-
dc.date.issued1982en_US
dc.identifier.citationBiochemical And Biophysical Research Communications, 1982, v. 109 n. 2, p. 305-312en_US
dc.identifier.issn0006-291Xen_US
dc.identifier.urihttp://hdl.handle.net/10722/147731-
dc.description.abstractMitochondrial δ-aminolaevulinate synthase was purified from drug-induced adult rat liver and identified for the first time as a protein of minimum molecular weight 70,000. The enzyme was also identified in mitochondria by pulse-labelling and immunoprecipitation and shown to have a molecular weight of 70,000. The purified enzyme was degraded by papain to smaller forms of molecular weight about 56,000 with no loss of enzyme activity. In vitro translation experiments suggest that the enzyme is synthesized initially as a larger precursor of molecular weight 76,000. © 1982.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/descriptionen_US
dc.relation.ispartofBiochemical and Biophysical Research Communicationsen_US
dc.subject.mesh5-Aminolevulinate Synthetase - Genetics - Isolation & Purification - Metabolismen_US
dc.subject.meshAnimalsen_US
dc.subject.meshMaleen_US
dc.subject.meshMitochondria, Liver - Enzymologyen_US
dc.subject.meshMolecular Weighten_US
dc.subject.meshPlants - Metabolismen_US
dc.subject.meshPoly A - Geneticsen_US
dc.subject.meshProtein Biosynthesisen_US
dc.subject.meshRna - Geneticsen_US
dc.subject.meshRna, Messengeren_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Inbred Strainsen_US
dc.subject.meshTriticum - Metabolismen_US
dc.titlePurification of rat liver mitochondrial δ-aminolaevulinate synthaseen_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.pmid6185121en_US
dc.identifier.scopuseid_2-s2.0-0020494194en_US
dc.identifier.volume109en_US
dc.identifier.issue2en_US
dc.identifier.spage305en_US
dc.identifier.epage312en_US
dc.identifier.isiWOS:A1982PS01300002-
dc.publisher.placeUnited Statesen_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats