Unidentified N-glycans by N-glycosidase A were Identified by N-glycosidase F under Denaturing Conditions in Plant Glycoprotein
DC Field | Value | Language |
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dc.contributor.author | Kim, Jeongeun | - |
dc.contributor.author | Kim, Jihye | - |
dc.contributor.author | Ryu, Changsoo | - |
dc.contributor.author | Lee, Jaeryong | - |
dc.contributor.author | Park, Chi Soo | - |
dc.contributor.author | Jin, Mijung | - |
dc.contributor.author | Kang, Minju | - |
dc.contributor.author | Kim, Ahyon | - |
dc.contributor.author | Mun, Chulmin | - |
dc.contributor.author | Kim, Ha Hyung | - |
dc.date.accessioned | 2023-02-19T17:40:34Z | - |
dc.date.available | 2023-02-19T17:40:34Z | - |
dc.date.issued | 2022 | - |
dc.identifier.issn | 0929-8665 | - |
dc.identifier.issn | 1875-5305 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/60762 | - |
dc.description.abstract | Background: The identification of N-glycans in plant glycoproteins or plant-made pharmaceuticals is essential for understanding their structure, function, properties, immunogenicity, and allergenicity (induced by plant-specific core-fucosylation or xylosylation) in the applications of plant food, agriculture, and plant biotechnology. N-glycosidase A is widely used to release the N-glycans of plant glycoproteins because the core-fucosylated N-glycans of plant glycoproteins are hydrolyzed by N-glycosidase A but not by N-glycosidase F. However, the efficiency of N-glycosidase A activity in plant glycoproteins remains unclear. Objective: The aim of the study was to elucidate the efficient use of N-glycosidases to identify and quantify the N-glycans of plant glycoproteins; it aimed at identification of released N-glycans by N-glycosidase F and assessment of their relative quantities with a focus on unidentified N-glycans by N-glycosidase A in plant glycoproteins, Phaseolus vulgaris lectin (PHA) and horseradish peroxidase (HRP). Methods: Liquid chromatography–tandem mass spectrometry was used to analyze and compare the N-glycans of PHA and HRP treated with either N-glycosidase A or F under denaturing conditions. The relative quantities (%) of each N-glycan (>0.1%) to the total N-glycans (100%) were determined. Results: N-glycosidase A and F released 9 identical N-glycans of PHA, but two additional core-fucosylated N-glycans were released by only N-glycosidase A, as expected. By contrast, in HRP, 8 N-glycans comprising 6 core-fucosylated N-glycans, 1 xylosylated N-glycan, and 1 mannosylated N-glycan were released by N-glycosidase A. Moreover, 8 unexpected N-glycans comprising 1 core-fucosylated N-glycan, 4 xylosylated N-glycans, and 3 mannosylated N-glycans were released by N-glycosidase F. Of these, 3 xylosylated and 2 mannosylated N-glycans were released by only N-glycansodase F. Conclusion: These results demonstrate that N-glycosidase A alone is insufficient to release the N-glycans of all plant glycoproteins, suggesting that to identify and quantify the released N-glycans of the plant glycoprotein HRP, both N-glycosidase A and F treatments are required. © 2022 Bentham Science Publishers. | - |
dc.format.extent | 8 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | Bentham Science Publishers | - |
dc.title | Unidentified N-glycans by N-glycosidase A were Identified by N-glycosidase F under Denaturing Conditions in Plant Glycoprotein | - |
dc.type | Article | - |
dc.identifier.doi | 10.2174/0929866529666220328152941 | - |
dc.identifier.bibliographicCitation | Protein and Peptide Letters, v.29, no.5, pp 440 - 447 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.wosid | 000836190600008 | - |
dc.identifier.scopusid | 2-s2.0-85132435188 | - |
dc.citation.endPage | 447 | - |
dc.citation.number | 5 | - |
dc.citation.startPage | 440 | - |
dc.citation.title | Protein and Peptide Letters | - |
dc.citation.volume | 29 | - |
dc.type.docType | Article | - |
dc.publisher.location | 아랍에미리트 | - |
dc.subject.keywordAuthor | Allergenicity | - |
dc.subject.keywordAuthor | mammalian cell cultures | - |
dc.subject.keywordAuthor | N-glycan | - |
dc.subject.keywordAuthor | N-glycosidase | - |
dc.subject.keywordAuthor | plant biotechnology | - |
dc.subject.keywordAuthor | plant glycoprotein | - |
dc.subject.keywordPlus | GLYCOSYLATION ANALYSIS | - |
dc.subject.keywordPlus | MASS-SPECTROMETRY | - |
dc.subject.keywordPlus | PHYTOHEMAGGLUTININ | - |
dc.subject.keywordPlus | PROCAINAMIDE | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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