Peptide-N-glycosidase F or A treatment and procainamide-labeling for identification and quantification of N-glycans in two types of mammalian glycoproteins using UPLC and LC-MS/MS
•Some reported N-glycan structures are inconsistent depending on the type of glycoprotein or the preparation methods.•N-glycans obtained by different preparation methods were compared with two types of mammalian glycoproteins.•N-glycans identified with PF-ProA or PA-ProA using LC-MS include those th...
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Published in | Journal of chromatography. B, Analytical technologies in the biomedical and life sciences Vol. 1214; p. 123538 |
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Main Authors | , , , , , , , , , , , |
Format | Journal Article |
Language | English |
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Elsevier B.V
01.01.2023
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Abstract | •Some reported N-glycan structures are inconsistent depending on the type of glycoprotein or the preparation methods.•N-glycans obtained by different preparation methods were compared with two types of mammalian glycoproteins.•N-glycans identified with PF-ProA or PA-ProA using LC-MS include those that cannot be identified by the widely used PF-AB.•Relative and absolute quantification of N-glycans was efficiently determined with PF-ProA or PA-ProA using UPLC and LC-MS.
N-glycans in glycoproteins can affect physicochemical properties of proteins; however, some reported N-glycan structures are inconsistent depending on the type of glycoprotein or the preparation methods.
To obtain consistent results for qualitative and quantitative analyses of N-glycans, N-glycans obtained by different preparation methods were compared for two types of mammalian glycoproteins.
N-glycans are released by peptide-N-glycosidase F (PF) or A (PA) from two model mammalian glycoproteins, bovine fetuin (with three glycosylation sites) and human IgG (with a single glycosylation site), and labeled with a fluorescent tag [2-aminobenzamide (AB) or procainamide (ProA)]. The structure and quantity of each N-glycan were determined using UPLC and LC-MS/MS.
The 21 N-glycans in fetuin and another 21 N-glycans in IgG by either PF-ProA or PA-ProA were identified using LC-MS/MS. The N-glycans in fetuin (8–13 N-glycans were previously reported) and in IgG (19 N-glycans were previously reported), which could not be identified by using the widely used PF-AB, were all identified by using PF-ProA or PA-ProA. The quantities (%) of the N-glycans (>0.1 %) relative to the total amount of N-glycans (100 %) obtained by AB- and ProA-labeling using LC-MS/MS had a similar tendency. However, the absolute quantities (pmol) of the N-glycans estimated using UPLC and LC-MS/MS were more efficiently determined with ProA-labeling than with AB-labeling. Thus, PF-ProA or PA-ProA allows for more effective identification and quantification of N-glycans than PF-AB in glycoprotein, particularly bovine fetuin. This study is the first comparative analysis for the identification and relative and absolute quantification of N-glycans in glycoproteins with PF-ProA and PA-ProA using UPLC and LC-MS/MS. |
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AbstractList | N-glycans in glycoproteins can affect physicochemical properties of proteins; however, some reported N-glycan structures are inconsistent depending on the type of glycoprotein or the preparation methods.
To obtain consistent results for qualitative and quantitative analyses of N-glycans, N-glycans obtained by different preparation methods were compared for two types of mammalian glycoproteins.
N-glycans are released by peptide-N-glycosidase F (PF) or A (PA) from two model mammalian glycoproteins, bovine fetuin (with three glycosylation sites) and human IgG (with a single glycosylation site), and labeled with a fluorescent tag [2-aminobenzamide (AB) or procainamide (ProA)]. The structure and quantity of each N-glycan were determined using UPLC and LC-MS/MS.
The 21 N-glycans in fetuin and another 21 N-glycans in IgG by either PF-ProA or PA-ProA were identified using LC-MS/MS. The N-glycans in fetuin (8-13 N-glycans were previously reported) and in IgG (19 N-glycans were previously reported), which could not be identified by using the widely used PF-AB, were all identified by using PF-ProA or PA-ProA. The quantities (%) of the N-glycans (>0.1 %) relative to the total amount of N-glycans (100 %) obtained by AB- and ProA-labeling using LC-MS/MS had a similar tendency. However, the absolute quantities (pmol) of the N-glycans estimated using UPLC and LC-MS/MS were more efficiently determined with ProA-labeling than with AB-labeling. Thus, PF-ProA or PA-ProA allows for more effective identification and quantification of N-glycans than PF-AB in glycoprotein, particularly bovine fetuin. This study is the first comparative analysis for the identification and relative and absolute quantification of N-glycans in glycoproteins with PF-ProA and PA-ProA using UPLC and LC-MS/MS. BACKGROUNDN-glycans in glycoproteins can affect physicochemical properties of proteins; however, some reported N-glycan structures are inconsistent depending on the type of glycoprotein or the preparation methods. OBJECTIVETo obtain consistent results for qualitative and quantitative analyses of N-glycans, N-glycans obtained by different preparation methods were compared for two types of mammalian glycoproteins. METHODSN-glycans are released by peptide-N-glycosidase F (PF) or A (PA) from two model mammalian glycoproteins, bovine fetuin (with three glycosylation sites) and human IgG (with a single glycosylation site), and labeled with a fluorescent tag [2-aminobenzamide (AB) or procainamide (ProA)]. The structure and quantity of each N-glycan were determined using UPLC and LC-MS/MS. RESULTSThe 21 N-glycans in fetuin and another 21 N-glycans in IgG by either PF-ProA or PA-ProA were identified using LC-MS/MS. The N-glycans in fetuin (8-13 N-glycans were previously reported) and in IgG (19 N-glycans were previously reported), which could not be identified by using the widely used PF-AB, were all identified by using PF-ProA or PA-ProA. The quantities (%) of the N-glycans (>0.1 %) relative to the total amount of N-glycans (100 %) obtained by AB- and ProA-labeling using LC-MS/MS had a similar tendency. However, the absolute quantities (pmol) of the N-glycans estimated using UPLC and LC-MS/MS were more efficiently determined with ProA-labeling than with AB-labeling. Thus, PF-ProA or PA-ProA allows for more effective identification and quantification of N-glycans than PF-AB in glycoprotein, particularly bovine fetuin. This study is the first comparative analysis for the identification and relative and absolute quantification of N-glycans in glycoproteins with PF-ProA and PA-ProA using UPLC and LC-MS/MS. •Some reported N-glycan structures are inconsistent depending on the type of glycoprotein or the preparation methods.•N-glycans obtained by different preparation methods were compared with two types of mammalian glycoproteins.•N-glycans identified with PF-ProA or PA-ProA using LC-MS include those that cannot be identified by the widely used PF-AB.•Relative and absolute quantification of N-glycans was efficiently determined with PF-ProA or PA-ProA using UPLC and LC-MS. N-glycans in glycoproteins can affect physicochemical properties of proteins; however, some reported N-glycan structures are inconsistent depending on the type of glycoprotein or the preparation methods. To obtain consistent results for qualitative and quantitative analyses of N-glycans, N-glycans obtained by different preparation methods were compared for two types of mammalian glycoproteins. N-glycans are released by peptide-N-glycosidase F (PF) or A (PA) from two model mammalian glycoproteins, bovine fetuin (with three glycosylation sites) and human IgG (with a single glycosylation site), and labeled with a fluorescent tag [2-aminobenzamide (AB) or procainamide (ProA)]. The structure and quantity of each N-glycan were determined using UPLC and LC-MS/MS. The 21 N-glycans in fetuin and another 21 N-glycans in IgG by either PF-ProA or PA-ProA were identified using LC-MS/MS. The N-glycans in fetuin (8–13 N-glycans were previously reported) and in IgG (19 N-glycans were previously reported), which could not be identified by using the widely used PF-AB, were all identified by using PF-ProA or PA-ProA. The quantities (%) of the N-glycans (>0.1 %) relative to the total amount of N-glycans (100 %) obtained by AB- and ProA-labeling using LC-MS/MS had a similar tendency. However, the absolute quantities (pmol) of the N-glycans estimated using UPLC and LC-MS/MS were more efficiently determined with ProA-labeling than with AB-labeling. Thus, PF-ProA or PA-ProA allows for more effective identification and quantification of N-glycans than PF-AB in glycoprotein, particularly bovine fetuin. This study is the first comparative analysis for the identification and relative and absolute quantification of N-glycans in glycoproteins with PF-ProA and PA-ProA using UPLC and LC-MS/MS. |
ArticleNumber | 123538 |
Author | Jang, Leeseul Kim, Ha Hyung Kim, Jeongeun Kim, Mirae Jang, Ji Yeon Kang, Minju Kim, Jieun Park, Chi Soo Moon, Chulmin Yang, Subin Kim, Ahyeon Jin, Mijung |
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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/36493594$$D View this record in MEDLINE/PubMed |
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CitedBy_id | crossref_primary_10_3390_ijms25031772 crossref_primary_10_1016_j_ijbiomac_2024_130836 crossref_primary_10_1002_pmic_202300281 crossref_primary_10_1016_j_abb_2024_110069 crossref_primary_10_1021_acsmeasuresciau_3c00071 crossref_primary_10_1016_j_cca_2024_117827 |
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Snippet | •Some reported N-glycan structures are inconsistent depending on the type of glycoprotein or the preparation methods.•N-glycans obtained by different... N-glycans in glycoproteins can affect physicochemical properties of proteins; however, some reported N-glycan structures are inconsistent depending on the type... BACKGROUNDN-glycans in glycoproteins can affect physicochemical properties of proteins; however, some reported N-glycan structures are inconsistent depending... |
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SubjectTerms | Animals Cattle Chromatography, Liquid - methods Glycoproteins - chemistry Humans Identification Immunoglobulin G - chemistry LC-MS/MS Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase N-glycan Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Peptides Polysaccharides - chemistry Procainamide - analysis Procainamide - chemistry Quantification Tandem Mass Spectrometry - methods Therapeutic glycoprotein UPLC |
Title | Peptide-N-glycosidase F or A treatment and procainamide-labeling for identification and quantification of N-glycans in two types of mammalian glycoproteins using UPLC and LC-MS/MS |
URI | https://dx.doi.org/10.1016/j.jchromb.2022.123538 https://www.ncbi.nlm.nih.gov/pubmed/36493594 https://search.proquest.com/docview/2753305216 |
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