File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Electron microscopic studies on liver 5-aminolaevulinate synthase.

TitleElectron microscopic studies on liver 5-aminolaevulinate synthase.
Authors
Pirola, BAMayer, FBorthwick, IASrivastava, GMay, BKElliott, WH
Issue Date1984
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EJB
Citation
European Journal Of Biochemistry, 1984, v. 144 n. 3, p. 577-579 How to Cite?
DOI: http://dx.doi.org/10.1111/j.1432-1033.1984.tb08504.x
AbstractThe structure of chick embryo liver 5-aminolaevulinate synthase has been examined by electron microscopic studies using negative staining. From the different projections of the enzyme particles observed in electron micrographs, a model for the enzyme molecule has been proposed. In this model, an enzyme molecule consists of two curved and identical subunits associated in opposite polarities. From the dimensions of an enzyme molecule subunit measured from electron micrographs, the relative molecular mass of each subunit is estimated to be 70 000.
Persistent Identifierhttp://hdl.handle.net/10722/147753
ISSN
0014-2956
ISI Accession Number ID
WOS:A1984TS08900024

 

DC FieldValueLanguage
dc.contributor.authorPirola, BAen_US
dc.contributor.authorMayer, Fen_US
dc.contributor.authorBorthwick, IAen_US
dc.contributor.authorSrivastava, Gen_US
dc.contributor.authorMay, BKen_US
dc.contributor.authorElliott, WHen_US
dc.date.accessioned2012-05-29T06:09:04Z-
dc.date.available2012-05-29T06:09:04Z-
dc.date.issued1984en_US
dc.identifier.citationEuropean Journal Of Biochemistry, 1984, v. 144 n. 3, p. 577-579en_US
dc.identifier.issn0014-2956en_US
dc.identifier.urihttp://hdl.handle.net/10722/147753-
dc.description.abstractThe structure of chick embryo liver 5-aminolaevulinate synthase has been examined by electron microscopic studies using negative staining. From the different projections of the enzyme particles observed in electron micrographs, a model for the enzyme molecule has been proposed. In this model, an enzyme molecule consists of two curved and identical subunits associated in opposite polarities. From the dimensions of an enzyme molecule subunit measured from electron micrographs, the relative molecular mass of each subunit is estimated to be 70 000.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 - Analysisen_US
dc.subject.meshAnimalsen_US
dc.subject.meshChick Embryoen_US
dc.subject.meshLiver - Enzymology - Ultrastructureen_US
dc.subject.meshMicroscopy, Electronen_US
dc.subject.meshModels, Structuralen_US
dc.titleElectron microscopic studies on liver 5-aminolaevulinate synthase.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.doi10.1111/j.1432-1033.1984.tb08504.x-
dc.identifier.pmid6489342-
dc.identifier.scopuseid_2-s2.0-0021753885en_US
dc.identifier.volume144en_US
dc.identifier.issue3en_US
dc.identifier.spage577en_US
dc.identifier.epage579en_US
dc.identifier.isiWOS:A1984TS08900024-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.issnl0014-2956-

Export via OAI-PMH Interface in XML Formats

OR

Export to Other Non-XML Formats