Show simple item record

dc.contributor.authorLin, Chi-Hung
dc.contributor.authorKuo, Chu-Wei
dc.contributor.authorJarvis, Donald L
dc.contributor.authorKhoo, Kay-Hooi
dc.date.accessioned2021-05-26T03:41:39Z
dc.date.available2021-05-26T03:41:39Z
dc.date.issued2014
dc.identifier.issn1615-9853en_US
dc.identifier.doi10.1002/pmic.201300343en_US
dc.identifier.urihttp://hdl.handle.net/10072/404694
dc.description.abstractThe relative amount of high mannose structures within an N-glycomic pool differs from one source to another, but quite often it predominates over the larger size complex type structures carrying biologically important glyco-epitopes. An efficient method to separate these two classes of N-glycans would significantly aid in detecting the lower abundant components by MS. Capitalizing on an initial observation that only high mannose type structures were recovered in the flow-through fraction when peptide-N-glycosidase F digested peptides were passed through a C18 cartridge in 0.1% formic acid, we demonstrated here that native complex type N-glycans can be retained by C18 cartridge and to be efficiently separated from both the smaller high mannose type structures, as well as de-N-glycosylated peptides by stepwise elution with increasing ACN concentration. The weak retention of the largely hydrophilic N-glycans on C18 resin is dependent not only on size but also increased by the presence of α6-fucosylation. This was shown by comparing the resulting N-glycomic profiles of the washed and low-ACN eluted fractions derived from both a human cancer cell line and an insect cell line.en_US
dc.description.peerreviewedYesen_US
dc.languageEnglishen_US
dc.publisherWileyen_US
dc.relation.ispartofpagefrom87en_US
dc.relation.ispartofpageto92en_US
dc.relation.ispartofissue1en_US
dc.relation.ispartofjournalProteomicsen_US
dc.relation.ispartofvolume14en_US
dc.subject.fieldofresearchBiological Sciencesen_US
dc.subject.fieldofresearchInformation and Computing Sciencesen_US
dc.subject.fieldofresearchMedical and Health Sciencesen_US
dc.subject.fieldofresearchcode06en_US
dc.subject.fieldofresearchcode08en_US
dc.subject.fieldofresearchcode11en_US
dc.subject.keywordsScience & Technologyen_US
dc.subject.keywordsLife Sciences & Biomedicineen_US
dc.subject.keywordsBiochemical Research Methodsen_US
dc.subject.keywordsBiochemistry & Molecular Biologyen_US
dc.subject.keywordsC18 RP SPEen_US
dc.titleFacile removal of high mannose structures prior to extracting complex type N-glycans from de-N-glycosylated peptides retained by C18 solid phase to allow more efficient glycomic mappingen_US
dc.typeJournal articleen_US
dc.type.descriptionC1 - Articlesen_US
dcterms.bibliographicCitationLin, C-H; Kuo, C-W; Jarvis, DL; Khoo, K-H, Facile removal of high mannose structures prior to extracting complex type N-glycans from de-N-glycosylated peptides retained by C18 solid phase to allow more efficient glycomic mapping, PROTEOMICS, 2014, 14 (1), pp. 87-92en_US
dcterms.dateAccepted2013-10-23
dc.date.updated2021-05-26T03:34:38Z
dc.description.versionAccepted Manuscript (AM)en_US
gro.rights.copyright© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. This is the peer reviewed version of the following article: Pacile removal of high mannose structures prior to extracting complex type N-glycans from de-N-glycosylated peptides retained by C18 solid phase to allow more efficient glycomic mapping, Proteomics, 2014, 14 (1), pp. 87-92, which has been published in final form at https://doi.org/10.1002/pmic.201300343. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving (http://olabout.wiley.com/WileyCDA/Section/id-828039.html)en_US
gro.hasfulltextFull Text
gro.griffith.authorLin, Chi-Hung


Files in this item

This item appears in the following Collection(s)

  • Journal articles
    Contains articles published by Griffith authors in scholarly journals.

Show simple item record