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Mass spectrometry in the determination of glycosylation site and N-glycan structures of human placental alkaline phosphatase

ArticleAçık Erişim

Özet

Alkaline phosphatase (AP) is a membrane-bound glycoprotein that is widely distributed in the plasma membrane of cells of various organs and also found in many organisms from bacteria to humans. The complete amino acid sequence and three-dimensional structure of human placental alkaline phosphatase have been reported. Based on the literature data, AP consists of two presumptive glycosylation sites, at Asn-144 and Asn-271. However, it only contains a single occupied N-linked glycosylation site and no occupied O-linked glycosylation sites. Hydrophilic interaction chromatography (HILIC) has been primarily employed for the characterization of the glycan structures derived from glycoproteins. N-glycan structures from human placental alkaline phosphatase (PLAP) were investigated using HILIC-Orbitrap MS, and subsequent data processing and glycan assignment software. 16 structures including 10 sialylated N-glycans were identified from PLAP. © Korean Society for Mass Spectrometry.

Anahtar Kelimeler

Alkaline phosphataseGlycosylationHILICMass spectrometryN-glycans
RDL Kalıcı Bağlantı (PID)
https://rdlopen.rawdatalibrary.net/r/ebyu/14367Resmi atıflarda kullanılan kalıcı adres
DOI
https://doi.org/10.5478/msl.2018.9.3.67Yayıncı resmi DOI adresi
Tam Kayıt
AlanDeğerDil
dc.contributor.authorSolakyildirim, Kemal
dc.contributor.authorLi, Lingyun
dc.contributor.authorLinhardt, Robert J.
dc.date.accessioned2026-10-18T20:29:09.652480032Z
dc.date.available2026-10-18T20:29:09.652480032Z
dc.date.issued2018
dc.description.abstractAlkaline phosphatase (AP) is a membrane-bound glycoprotein that is widely distributed in the plasma membrane of cells of various organs and also found in many organisms from bacteria to humans. The complete amino acid sequence and three-dimensional structure of human placental alkaline phosphatase have been reported. Based on the literature data, AP consists of two presumptive glycosylation sites, at Asn-144 and Asn-271. However, it only contains a single occupied N-linked glycosylation site and no occupied O-linked glycosylation sites. Hydrophilic interaction chromatography (HILIC) has been primarily employed for the characterization of the glycan structures derived from glycoproteins. N-glycan structures from human placental alkaline phosphatase (PLAP) were investigated using HILIC-Orbitrap MS, and subsequent data processing and glycan assignment software. 16 structures including 10 sialylated N-glycans were identified from PLAP. © Korean Society for Mass Spectrometry.
dc.description.sponsorshipThis work was supported by the US National Institute of Health (grant number HL096972).
dc.identifier.doi10.5478/msl.2018.9.3.67
dc.identifier.eissn2093-8950
dc.identifier.endpage72
dc.identifier.issn2233-4203
dc.identifier.issue3
dc.identifier.scopus2-s2.0-85059133982
dc.identifier.startpage67
dc.identifier.urihttps://rdlopen.rawdatalibrary.net/r/ebyu/14367
dc.identifier.volume9
dc.identifier.wosWOS:000446543500001
dc.language.isoen
dc.publisherKorean Society for Mass Spectrometry
dc.relation.ispartofMass Spectrometry Letters
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectAlkaline phosphatase
dc.subjectGlycosylation
dc.subjectHILIC
dc.subjectMass spectrometry
dc.subjectN-glycans
dc.titleMass spectrometry in the determination of glycosylation site and N-glycan structures of human placental alkaline phosphatase
dc.typeArticle
dspace.entity.typePublication
rdl.citation.scopus5
rdl.citation.wos4
rdl.source.indexSCOPUS
rdl.source.indexWOS
rdl.wos.indexEmerging Sources Citation Index (ESCI)