File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Quantitation of type I and III collagens using electrophoresis of alpha chains and cyanogen bromide peptides

TitleQuantitation of type I and III collagens using electrophoresis of alpha chains and cyanogen bromide peptides
Authors
Issue Date1984
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yabio
Citation
Analytical Biochemistry, 1984, v. 139 n. 2, p. 322-328 How to Cite?
AbstractThe methods of quantitating the relative amounts of type I and III collagens in samples containing crosslinked collagen chains were evaluated using electrophoresis of alpha chains and cyanogen bromide peptides. The densitometry areas of the αI(I) chains from type I collagen and the αI(III) chains from type III collagen were reduced because of the failure of the crosslinked chains to dissociate. However, the ratios of the unit densitometry areas of these chains (area of chain/μg type I or III collagen loaded) were constant for type I and III collagens prepared from the same samples of tissue. A calibration factor, which was the same for dermis and mitral valve, was derived to convert the densitometry areas of the αI(I) CB8 (type I collagen marker) and the αI(III) CB5 (type III collagen marker) were not reduced by crosslinked collagen chains. A calibration factor was also derived to convert the ratios of the densitometry areas of the marker peptides to weight ratios of type I or III collagens. Almost identical results were obtained when electrophoresis of alpha chains and of cyanogen bromide peptides was used with these calibration factors that quantitate the relative amounts of type I and III collagens in tissue extracts which contained different amounts of crosslinked chains.
Persistent Identifierhttp://hdl.handle.net/10722/147306
ISSN
2015 Impact Factor: 2.243
2015 SCImago Journal Rankings: 0.725
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorChan, Den_US
dc.contributor.authorCole, WGen_US
dc.date.accessioned2012-05-29T06:02:49Z-
dc.date.available2012-05-29T06:02:49Z-
dc.date.issued1984en_US
dc.identifier.citationAnalytical Biochemistry, 1984, v. 139 n. 2, p. 322-328en_US
dc.identifier.issn0003-2697en_US
dc.identifier.urihttp://hdl.handle.net/10722/147306-
dc.description.abstractThe methods of quantitating the relative amounts of type I and III collagens in samples containing crosslinked collagen chains were evaluated using electrophoresis of alpha chains and cyanogen bromide peptides. The densitometry areas of the αI(I) chains from type I collagen and the αI(III) chains from type III collagen were reduced because of the failure of the crosslinked chains to dissociate. However, the ratios of the unit densitometry areas of these chains (area of chain/μg type I or III collagen loaded) were constant for type I and III collagens prepared from the same samples of tissue. A calibration factor, which was the same for dermis and mitral valve, was derived to convert the densitometry areas of the αI(I) CB8 (type I collagen marker) and the αI(III) CB5 (type III collagen marker) were not reduced by crosslinked collagen chains. A calibration factor was also derived to convert the ratios of the densitometry areas of the marker peptides to weight ratios of type I or III collagens. Almost identical results were obtained when electrophoresis of alpha chains and of cyanogen bromide peptides was used with these calibration factors that quantitate the relative amounts of type I and III collagens in tissue extracts which contained different amounts of crosslinked chains.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yabioen_US
dc.relation.ispartofAnalytical Biochemistryen_US
dc.subject.meshChild, Preschoolen_US
dc.subject.meshCollagen - Analysis - Classificationen_US
dc.subject.meshCyanogen Bromideen_US
dc.subject.meshDensitometryen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshHumansen_US
dc.subject.meshMaleen_US
dc.subject.meshMiddle Ageden_US
dc.subject.meshPeptide Fragments - Analysisen_US
dc.subject.meshSkin - Analysisen_US
dc.titleQuantitation of type I and III collagens using electrophoresis of alpha chains and cyanogen bromide peptidesen_US
dc.typeArticleen_US
dc.identifier.emailChan, D:chand@hkucc.hku.hken_US
dc.identifier.authorityChan, D=rp00540en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid6476370-
dc.identifier.scopuseid_2-s2.0-0021227948en_US
dc.identifier.volume139en_US
dc.identifier.issue2en_US
dc.identifier.spage322en_US
dc.identifier.epage328en_US
dc.identifier.isiWOS:A1984SX64400012-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridCole, WG=7201518727en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats