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Article: Rapid fractionation of collagen chains and peptides by high-performance liquid chromatography

TitleRapid fractionation of collagen chains and peptides by high-performance liquid chromatography
Authors
Issue Date1986
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yabio
Citation
Analytical Biochemistry, 1986, v. 154 n. 1, p. 338-344 How to Cite?
AbstractA strategy was developed, using a Pharmacia Fast Protein Liquid chromatography (FPLC) system, for the rapid preparation of the α-chains, cyanogen bromide peptides and tryptic peptides of type I collagen obtained from tissues and cultured fibroblasts. Collagen α-chains were prepared using a C18 PEP-RPC reverse-phase column and volatile solvents. Preliminary Superose 6 gel permeation chromatography was used to separate the crosslinked β- and γ-chains from the α-chains of tissue collagen samples. A Mono S cation-exchange column was used to resolve all of the major type I collagen cyanogen bromide peptides including the α1(I)CB7 and CB8 peptides, which have not been well resolved by previously published methods. Collagen tryptic peptides were chromatographed on the PEP-RPC reverse-phase column.
Persistent Identifierhttp://hdl.handle.net/10722/147317
ISSN
2015 Impact Factor: 2.243
2015 SCImago Journal Rankings: 0.725
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorBateman, JFen_US
dc.contributor.authorMascara, Ten_US
dc.contributor.authorChan, Den_US
dc.contributor.authorCole, WGen_US
dc.date.accessioned2012-05-29T06:02:53Z-
dc.date.available2012-05-29T06:02:53Z-
dc.date.issued1986en_US
dc.identifier.citationAnalytical Biochemistry, 1986, v. 154 n. 1, p. 338-344en_US
dc.identifier.issn0003-2697en_US
dc.identifier.urihttp://hdl.handle.net/10722/147317-
dc.description.abstractA strategy was developed, using a Pharmacia Fast Protein Liquid chromatography (FPLC) system, for the rapid preparation of the α-chains, cyanogen bromide peptides and tryptic peptides of type I collagen obtained from tissues and cultured fibroblasts. Collagen α-chains were prepared using a C18 PEP-RPC reverse-phase column and volatile solvents. Preliminary Superose 6 gel permeation chromatography was used to separate the crosslinked β- and γ-chains from the α-chains of tissue collagen samples. A Mono S cation-exchange column was used to resolve all of the major type I collagen cyanogen bromide peptides including the α1(I)CB7 and CB8 peptides, which have not been well resolved by previously published methods. Collagen tryptic peptides were chromatographed on the PEP-RPC reverse-phase column.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.meshCells, Cultureden_US
dc.subject.meshChromatography, High Pressure Liquid - Methodsen_US
dc.subject.meshCollagen - Isolation & Purificationen_US
dc.subject.meshCyanogen Bromideen_US
dc.subject.meshFibroblasts - Analysisen_US
dc.subject.meshHumansen_US
dc.subject.meshPeptide Fragments - Isolation & Purificationen_US
dc.subject.meshSkin - Analysisen_US
dc.subject.meshTrypsinen_US
dc.titleRapid fractionation of collagen chains and peptides by high-performance liquid chromatographyen_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.pmid3706733-
dc.identifier.scopuseid_2-s2.0-0022510760en_US
dc.identifier.volume154en_US
dc.identifier.issue1en_US
dc.identifier.spage338en_US
dc.identifier.epage344en_US
dc.identifier.isiWOS:A1986A742800048-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridBateman, JF=16135557700en_US
dc.identifier.scopusauthoridMascara, T=6602227390en_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridCole, WG=7201518727en_US

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