Evaluation of Jacalin lectin sorbents for the extraction of the human chorionic gonadotropin glycoforms prior to analysis by nano liquid chromatography-high resolution mass spectrometry
Human chorionic gonadotropin (hCG) is a dimeric, highly glycosylated hormone with a total of 4 N- and 4 O-glycosylation sites in its two subunits, hCGα and hCGβ. Recently, we developed a novel nano liquid chromatography coupled to high resolution mass spectrometry (nanoLC-HRMS) method for the analys...
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| Vydané v: | Journal of pharmaceutical and biomedical analysis Ročník 252; s. 116525 |
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| Hlavní autori: | , , , , , |
| Médium: | Journal Article |
| Jazyk: | English |
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England
Elsevier B.V
01.01.2025
Elsevier |
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| ISSN: | 0731-7085, 1873-264X, 1873-264X |
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| Abstract | Human chorionic gonadotropin (hCG) is a dimeric, highly glycosylated hormone with a total of 4 N- and 4 O-glycosylation sites in its two subunits, hCGα and hCGβ. Recently, we developed a novel nano liquid chromatography coupled to high resolution mass spectrometry (nanoLC-HRMS) method for the analysis and thus the detection of the intact glycoforms of hCG. Here, a sorbent functionalized with the Jacalin lectin was evaluated in solid-phase extraction (SPE) for its potential to fractionate the hCG glycoforms prior to their nanoLC-HRMS analysis at the intact level, which may facilitate the detection of low-abundance glycoforms and may lead to a more detailed characterization of the hormone glycosylation. A commercial sorbent based on Jacalin immobilized on Sepharose and having a lectin density of 4.5 mg per ml of gel was selected to carry out SPE and its capacity was estimated to be of some tens of μg of hCG per ml of lectin sorbent. Next, the SPE protocol was modified to improve the extraction recoveries. Especially, it was noticed that an extensive pre-conditioning procedure prior to the first use of a cartridge was necessary to remove the residual non-grafted lectins. Indeed, if non-grafted lectins are not eliminated, they may bind a part of hCG glycoforms preventing their retention by the sorbent, leading to low extraction recoveries (around 10 %). With the extensive pre-conditioning procedure, the average extraction recoveries for both hCGα and hCGβ glycoforms were about 50 %, with either recombinant or urinary hCG. Qualitatively, the fractionation of hCG glycoforms between the washing and elution fractions was achieved with the urinary hCG sample by determining the number of glycoforms detected in each fraction. It appears that 12 hCGα glycoforms have a low affinity (detected only in the washing fraction), 1 a low-medium affinity (detected in washing and elution 1 fractions), 16 a medium affinity (detected in washing, elution 1 and 2 fractions), and 12 a high affinity (detected only in elution 1 and 2 fractions). For the hCGβ glycoforms, similarly, 3 have a low affinity and 12 a low-medium affinity. Additionally, the 3 hCGβ glycoforms were detected better. A different behavior was observed with the recombinant hCG sample, which indicates glycosylation differences between the two hCG samples. This shows the potential of lectin-based affinity fractionation before nanoLC-HRMS analysis to better characterize the glycosylation state of hCG at the intact level.
•Capacity of Jacalin sorbents were evaluated with recombinant and urinary hCG.•the SPE procedure was developed to improve extraction recoveries.•SPE with Jacalin sorbents led to recoveries of around 50 % for hCG glycoforms.•Jacalin SPE enabled fractionation of hCG glycoforms as a function of their affinity.•lectin SPE and intact protein analysis by nanoLC-HRMS improves hCG characterization. |
|---|---|
| AbstractList | Human chorionic gonadotropin (hCG) is a dimeric, highly glycosylated hormone with a total of 4 N- and 4 O-glycosylation sites in its two subunits, hCGα and hCGβ. Recently, we developed a novel nano liquid chromatography coupled to high resolution mass spectrometry (nanoLC-HRMS) method for the analysis and thus the detection of the intact glycoforms of hCG. Here, a sorbent functionalized with the Jacalin lectin was evaluated in solid-phase extraction (SPE) for its potential to fractionate the hCG glycoforms prior to their nanoLC-HRMS analysis at the intact level, which may facilitate the detection of low-abundance glycoforms and may lead to a more detailed characterization of the hormone glycosylation. A commercial sorbent based on Jacalin immobilized on Sepharose and having a lectin density of 4.5 mg per ml of gel was selected to carry out SPE and its capacity was estimated to be of some tens of μg of hCG per ml of lectin sorbent. Next, the SPE protocol was modified to improve the extraction recoveries. Especially, it was noticed that an extensive pre-conditioning procedure prior to the first use of a cartridge was necessary to remove the residual non-grafted lectins. Indeed, if on-grafted lectins are not eliminated, they may bind a part of hCG glycoformes preventing they retention by the sorbent, leading to low extraction recoveries (around 10%). With the extensive pre-conditioning procedure, the average extraction recoveries for both hCGα and hCGβ glycoforms were about 50%, with either recombinant or urinary hCG. Qualitatively, the fractionation of hCG glycoforms between the washing and elution fractions was achieved with the urinary hCG sample by determining the number of glycoforms detected in each fraction. It appears that 12 hCGα glycoforms have a low affinity (detected only in the washing fraction), 1 a low-medium affinity (detected in washing and elution 1 fractions), 16 a medium affinity (detected in washing, elution 1 and 2 fractions), and 12 a high affinity (detected only in elution 1 and 2 fractions). For the hCGβ glycoforms, similarly, 3 have a low affinity and 12 a low-medium affinity. Additionally, the 3 hCGβ glycoforms were detected better. A different behavior was observed with the recombinant hCG sample, which indicates glycosylation differences between the two hCG samples. This shows the potential of lectin-based affinity fractionation before nanoLC-HRMS analysis to better characterize the glycosylation state of hCG at the intact level. Human chorionic gonadotropin (hCG) is a dimeric, highly glycosylated hormone with a total of 4 N- and 4 O-glycosylation sites in its two subunits, hCGα and hCGβ. Recently, we developed a novel nano liquid chromatography coupled to high resolution mass spectrometry (nanoLC-HRMS) method for the analysis and thus the detection of the intact glycoforms of hCG. Here, a sorbent functionalized with the Jacalin lectin was evaluated in solid-phase extraction (SPE) for its potential to fractionate the hCG glycoforms prior to their nanoLC-HRMS analysis at the intact level, which may facilitate the detection of low-abundance glycoforms and may lead to a more detailed characterization of the hormone glycosylation. A commercial sorbent based on Jacalin immobilized on Sepharose and having a lectin density of 4.5 mg per ml of gel was selected to carry out SPE and its capacity was estimated to be of some tens of μg of hCG per ml of lectin sorbent. Next, the SPE protocol was modified to improve the extraction recoveries. Especially, it was noticed that an extensive pre-conditioning procedure prior to the first use of a cartridge was necessary to remove the residual non-grafted lectins. Indeed, if non-grafted lectins are not eliminated, they may bind a part of hCG glycoforms preventing their retention by the sorbent, leading to low extraction recoveries (around 10 %). With the extensive pre-conditioning procedure, the average extraction recoveries for both hCGα and hCGβ glycoforms were about 50 %, with either recombinant or urinary hCG. Qualitatively, the fractionation of hCG glycoforms between the washing and elution fractions was achieved with the urinary hCG sample by determining the number of glycoforms detected in each fraction. It appears that 12 hCGα glycoforms have a low affinity (detected only in the washing fraction), 1 a low-medium affinity (detected in washing and elution 1 fractions), 16 a medium affinity (detected in washing, elution 1 and 2 fractions), and 12 a high affinity (detected only in elution 1 and 2 fractions). For the hCGβ glycoforms, similarly, 3 have a low affinity and 12 a low-medium affinity. Additionally, the 3 hCGβ glycoforms were detected better. A different behavior was observed with the recombinant hCG sample, which indicates glycosylation differences between the two hCG samples. This shows the potential of lectin-based affinity fractionation before nanoLC-HRMS analysis to better characterize the glycosylation state of hCG at the intact level. •Capacity of Jacalin sorbents were evaluated with recombinant and urinary hCG.•the SPE procedure was developed to improve extraction recoveries.•SPE with Jacalin sorbents led to recoveries of around 50 % for hCG glycoforms.•Jacalin SPE enabled fractionation of hCG glycoforms as a function of their affinity.•lectin SPE and intact protein analysis by nanoLC-HRMS improves hCG characterization. Human chorionic gonadotropin (hCG) is a dimeric, highly glycosylated hormone with a total of 4 N- and 4 O-glycosylation sites in its two subunits, hCGα and hCGβ. Recently, we developed a novel nano liquid chromatography coupled to high resolution mass spectrometry (nanoLC-HRMS) method for the analysis and thus the detection of the intact glycoforms of hCG. Here, a sorbent functionalized with the Jacalin lectin was evaluated in solid-phase extraction (SPE) for its potential to fractionate the hCG glycoforms prior to their nanoLC-HRMS analysis at the intact level, which may facilitate the detection of low-abundance glycoforms and may lead to a more detailed characterization of the hormone glycosylation. A commercial sorbent based on Jacalin immobilized on Sepharose and having a lectin density of 4.5 mg per ml of gel was selected to carry out SPE and its capacity was estimated to be of some tens of μg of hCG per ml of lectin sorbent. Next, the SPE protocol was modified to improve the extraction recoveries. Especially, it was noticed that an extensive pre-conditioning procedure prior to the first use of a cartridge was necessary to remove the residual non-grafted lectins. Indeed, if non-grafted lectins are not eliminated, they may bind a part of hCG glycoforms preventing their retention by the sorbent, leading to low extraction recoveries (around 10 %). With the extensive pre-conditioning procedure, the average extraction recoveries for both hCGα and hCGβ glycoforms were about 50 %, with either recombinant or urinary hCG. Qualitatively, the fractionation of hCG glycoforms between the washing and elution fractions was achieved with the urinary hCG sample by determining the number of glycoforms detected in each fraction. It appears that 12 hCGα glycoforms have a low affinity (detected only in the washing fraction), 1 a low-medium affinity (detected in washing and elution 1 fractions), 16 a medium affinity (detected in washing, elution 1 and 2 fractions), and 12 a high affinity (detected only in elution 1 and 2 fractions). For the hCGβ glycoforms, similarly, 3 have a low affinity and 12 a low-medium affinity. Additionally, the 3 hCGβ glycoforms were detected better. A different behavior was observed with the recombinant hCG sample, which indicates glycosylation differences between the two hCG samples. This shows the potential of lectin-based affinity fractionation before nanoLC-HRMS analysis to better characterize the glycosylation state of hCG at the intact level.Human chorionic gonadotropin (hCG) is a dimeric, highly glycosylated hormone with a total of 4 N- and 4 O-glycosylation sites in its two subunits, hCGα and hCGβ. Recently, we developed a novel nano liquid chromatography coupled to high resolution mass spectrometry (nanoLC-HRMS) method for the analysis and thus the detection of the intact glycoforms of hCG. Here, a sorbent functionalized with the Jacalin lectin was evaluated in solid-phase extraction (SPE) for its potential to fractionate the hCG glycoforms prior to their nanoLC-HRMS analysis at the intact level, which may facilitate the detection of low-abundance glycoforms and may lead to a more detailed characterization of the hormone glycosylation. A commercial sorbent based on Jacalin immobilized on Sepharose and having a lectin density of 4.5 mg per ml of gel was selected to carry out SPE and its capacity was estimated to be of some tens of μg of hCG per ml of lectin sorbent. Next, the SPE protocol was modified to improve the extraction recoveries. Especially, it was noticed that an extensive pre-conditioning procedure prior to the first use of a cartridge was necessary to remove the residual non-grafted lectins. Indeed, if non-grafted lectins are not eliminated, they may bind a part of hCG glycoforms preventing their retention by the sorbent, leading to low extraction recoveries (around 10 %). With the extensive pre-conditioning procedure, the average extraction recoveries for both hCGα and hCGβ glycoforms were about 50 %, with either recombinant or urinary hCG. Qualitatively, the fractionation of hCG glycoforms between the washing and elution fractions was achieved with the urinary hCG sample by determining the number of glycoforms detected in each fraction. It appears that 12 hCGα glycoforms have a low affinity (detected only in the washing fraction), 1 a low-medium affinity (detected in washing and elution 1 fractions), 16 a medium affinity (detected in washing, elution 1 and 2 fractions), and 12 a high affinity (detected only in elution 1 and 2 fractions). For the hCGβ glycoforms, similarly, 3 have a low affinity and 12 a low-medium affinity. Additionally, the 3 hCGβ glycoforms were detected better. A different behavior was observed with the recombinant hCG sample, which indicates glycosylation differences between the two hCG samples. This shows the potential of lectin-based affinity fractionation before nanoLC-HRMS analysis to better characterize the glycosylation state of hCG at the intact level. Human chorionic gonadotropin (hCG) is a dimeric, highly glycosylated hormone with a total of 4 N- and 4 O-glycosylation sites in its two subunits, hCGα and hCGβ. Recently, we developed a novel nano liquid chromatography coupled to high resolution mass spectrometry (nanoLC-HRMS) method for the analysis and thus the detection of the intact glycoforms of hCG. Here, a sorbent functionalized with the Jacalin lectin was evaluated in solid-phase extraction (SPE) for its potential to fractionate the hCG glycoforms prior to their nanoLC-HRMS analysis at the intact level, which may facilitate the detection of low-abundance glycoforms and may lead to a more detailed characterization of the hormone glycosylation. A commercial sorbent based on Jacalin immobilized on Sepharose and having a lectin density of 4.5 mg per ml of gel was selected to carry out SPE and its capacity was estimated to be of some tens of μg of hCG per ml of lectin sorbent. Next, the SPE protocol was modified to improve the extraction recoveries. Especially, it was noticed that an extensive pre-conditioning procedure prior to the first use of a cartridge was necessary to remove the residual non-grafted lectins. Indeed, if non-grafted lectins are not eliminated, they may bind a part of hCG glycoforms preventing their retention by the sorbent, leading to low extraction recoveries (around 10 %). With the extensive pre-conditioning procedure, the average extraction recoveries for both hCGα and hCGβ glycoforms were about 50 %, with either recombinant or urinary hCG. Qualitatively, the fractionation of hCG glycoforms between the washing and elution fractions was achieved with the urinary hCG sample by determining the number of glycoforms detected in each fraction. It appears that 12 hCGα glycoforms have a low affinity (detected only in the washing fraction), 1 a low-medium affinity (detected in washing and elution 1 fractions), 16 a medium affinity (detected in washing, elution 1 and 2 fractions), and 12 a high affinity (detected only in elution 1 and 2 fractions). For the hCGβ glycoforms, similarly, 3 have a low affinity and 12 a low-medium affinity. Additionally, the 3 hCGβ glycoforms were detected better. A different behavior was observed with the recombinant hCG sample, which indicates glycosylation differences between the two hCG samples. This shows the potential of lectin-based affinity fractionation before nanoLC-HRMS analysis to better characterize the glycosylation state of hCG at the intact level. |
| ArticleNumber | 116525 |
| Author | Goumenou, Anastasia Combès, Audrey Delaunay, Nathalie Chendo, Christophe Fournier, Thierry Pichon, Valérie |
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| Cites_doi | 10.1016/0006-291X(84)91228-2 10.1016/j.jpba.2019.112921 10.1016/j.jpba.2024.116022 10.1016/j.talanta.2019.120171 10.1016/j.chroma.2016.07.058 10.1016/j.molimm.2016.06.015 10.1016/j.chroma.2017.10.033 10.1002/pd.507 10.1074/jbc.M115.657072 10.1507/endocrj1954.32.463 10.1016/0005-2795(80)90130-0 10.3892/or.2014.2979 10.1016/j.talanta.2018.09.095 10.1016/j.fertnstert.2008.08.031 10.1093/glycob/cwj038 10.1016/0003-2697(90)90605-9 10.1016/j.mce.2006.05.010 10.1016/0021-9673(92)80101-Y 10.1159/000217896 10.1093/molehr/gax047 10.1007/s00216-020-02684-8 10.1016/j.chroma.2006.07.070 10.2147/BTT.S141203 10.1007/s00216-014-8439-7 10.1016/j.chroma.2021.461945 10.3390/molecules21111577 10.1007/s00216-020-02794-3 10.1016/j.cca.2011.09.037 10.3389/fendo.2019.00503 10.1021/ac901506p 10.1016/j.ab.2008.12.005 10.1371/journal.pone.0228507 10.1093/glycob/cwl034 10.1016/j.placenta.2015.02.002 10.1016/S0925-4439(99)00060-5 |
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| Keywords | Jacalin Lectin Solid phase extraction Liquid chromatography Mass spectrometry Human chorionic gonadotropin mass spectrometry liquid chromatography human chorionic gonadotropin solid phase extraction lectin |
| Language | English |
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| References | Thakur, Rejtar, Karger, Washburn, Bosques, Gunay, Shriver, Venkataraman (bib13) 2009; 81 Valmu, Alfthan, Hotakainen, Birken, Stenman (bib2) 2006; 16 Li, Zhang, Li, Chi, Zhu, Zhang, Chi (bib7) 2015; 290 Camperi, Pichon, Delaunay (bib15) 2020; 178 Talbot, Spencer, Abushoufa (bib5) 2003; 23 Berger, Lapthorn (bib30) 2016; 76 Ek, Gianazza, Righetti (bib32) 1980; 626 Nishimura, Utsunomiya, Ide, Tanabe, Hamamoto, Mochizuki (bib34) 1985; 32 Fournier, Guibourdenche, Evain-Brion (bib1) 2015; 36 Kobata, Takeuchi (bib4) 1999; 1455 Camperi, De Cock, Pichon, Combes, Guibourdenche, Fournier, Vander Heyden, Mangelings, Delaunay (bib14) 2019; 193 Ibeto, Antonopoulos, Grassi, Pang, Panico, Bobdiwala, Al-Memar, Davis, Davis, Taylor, Almeida, Johnson, Harvey, Bourne, Seckl, Clark, Haslam, Dell (bib9) 2020; 15 Hortin, Trimpe (bib26) 1990; 188 Kobayashi, Masuda, Banno, Kobayashi, Umene, Nogami, Tsuji, Ueki, Nomura, Sato, Tominaga, Shimizu, Saya, Aoki (bib21) 2014; 31 Perchepied, Eskenazi, Giangrande, Camperi, Fournier, Vinh, Delaunay, Pichon (bib8) 2020; 206 Al Matari, Goumenou, Combès, Fournier, Pichon, Delaunay (bib16) 2021; 1640 Durham, Regnier (bib25) 2006; 1132 Iskratsch, Braun, Paschinger, Wilson (bib17) 2009; 386 Practice Committee of American Society for Reproductive Medicine, Birmingham, Alabama, Gonadotropin preparations: past, present, and future perspectives. Fertil. Steril. 90 (2008) S13-S20. https://doi.org/10.1016/j.fertnstert.2008.08.031 . Goumenou, Chendo, Combès, Fournier, Pichon, Delaunay (bib29) 2024; 242 Bonichon, Combès, Desoubries, Bossée, Pichon (bib31) 2016; 1461 Camperi, Combès, Fournier, Pichon, Delaunay (bib12) 2020; 412 Cole (bib3) 2012; 413 Al Matari, Combès, Camperi, Fournier, Pichon, Delaunay (bib11) 2020; 412 Bonichon, Combès, Desoubries, Bossée, Pichon (bib33) 2017; 1526 Kobata, Endo (bib22) 1992; 597 Zucca, Fernandez-Lafuente, Sanjust (bib23) 2016; 21 Riccetti, Klett, Ayoub, Boulo, Pignatti, Tagliavini, Varani, Trenti, Nicoli, Capodanno, La Sala, Reiter, Simoni, Casarini (bib18) 2017; 23 Kelly, Birken, Puett (bib20) 2007; 260-262 Cole, Perini, Birken, Ruddon (bib35) 1984; 122 Riccetti, Sperduti, Lazzaretti, Klett, De Pascali, Paradiso, Limoncella, Potì, Tagliavini, Trenti, Galano, Palmese, Satwekar, Daolio, Nicoli, Villani, Aguzzoli, Reiter, Simoni, Casarini (bib19) 2019; 10 Thennati, Singh, Nage, Patel, Bose, Burade, Ranbhor (bib10) 2018; 12 Tachibana, Nakamura, Wang, Iwasaki, Tachibana, Maebara, Cheng, Hirabayashi, Narimatsu (bib24) 2006; 16 Sakai, Yamagishi, Miura, Hata, Koyama, Sakagishi, Komoda (bib27) 1994; 15 Bai, Li, Zhu, Guan, Zhang, Chi (bib28) 2015; 407 Fournier (10.1016/j.jpba.2024.116525_bib1) 2015; 36 Thakur (10.1016/j.jpba.2024.116525_bib13) 2009; 81 Camperi (10.1016/j.jpba.2024.116525_bib12) 2020; 412 Camperi (10.1016/j.jpba.2024.116525_bib14) 2019; 193 Kobata (10.1016/j.jpba.2024.116525_bib4) 1999; 1455 Riccetti (10.1016/j.jpba.2024.116525_bib18) 2017; 23 Ibeto (10.1016/j.jpba.2024.116525_bib9) 2020; 15 Bonichon (10.1016/j.jpba.2024.116525_bib33) 2017; 1526 Kelly (10.1016/j.jpba.2024.116525_bib20) 2007; 260-262 Valmu (10.1016/j.jpba.2024.116525_bib2) 2006; 16 Nishimura (10.1016/j.jpba.2024.116525_bib34) 1985; 32 Cole (10.1016/j.jpba.2024.116525_bib35) 1984; 122 Cole (10.1016/j.jpba.2024.116525_bib3) 2012; 413 Camperi (10.1016/j.jpba.2024.116525_bib15) 2020; 178 Talbot (10.1016/j.jpba.2024.116525_bib5) 2003; 23 Bai (10.1016/j.jpba.2024.116525_bib28) 2015; 407 Kobayashi (10.1016/j.jpba.2024.116525_bib21) 2014; 31 Kobata (10.1016/j.jpba.2024.116525_bib22) 1992; 597 Ek (10.1016/j.jpba.2024.116525_bib32) 1980; 626 Hortin (10.1016/j.jpba.2024.116525_bib26) 1990; 188 Iskratsch (10.1016/j.jpba.2024.116525_bib17) 2009; 386 Durham (10.1016/j.jpba.2024.116525_bib25) 2006; 1132 10.1016/j.jpba.2024.116525_bib6 Tachibana (10.1016/j.jpba.2024.116525_bib24) 2006; 16 Thennati (10.1016/j.jpba.2024.116525_bib10) 2018; 12 Al Matari (10.1016/j.jpba.2024.116525_bib11) 2020; 412 Riccetti (10.1016/j.jpba.2024.116525_bib19) 2019; 10 Zucca (10.1016/j.jpba.2024.116525_bib23) 2016; 21 Bonichon (10.1016/j.jpba.2024.116525_bib31) 2016; 1461 Goumenou (10.1016/j.jpba.2024.116525_bib29) 2024; 242 Al Matari (10.1016/j.jpba.2024.116525_bib16) 2021; 1640 Perchepied (10.1016/j.jpba.2024.116525_bib8) 2020; 206 Li (10.1016/j.jpba.2024.116525_bib7) 2015; 290 Berger (10.1016/j.jpba.2024.116525_bib30) 2016; 76 Sakai (10.1016/j.jpba.2024.116525_bib27) 1994; 15 |
| References_xml | – volume: 1526 start-page: 70 year: 2017 end-page: 81 ident: bib33 article-title: Development of immunosorbents coupled on-line to immobilized pepsin reactor and micro liquid chromatography–tandem mass spectrometry for analysis of butyrylcholinesterase in human plasma publication-title: J. Chromatogr. A – volume: 23 start-page: 1 year: 2003 end-page: 5 ident: bib5 article-title: Detection of maternal serum hCG glycoform variants in the second trimester of pregnancies affected by down syndrome using a lectin immunoassay publication-title: Prenat. Diagn. – volume: 290 start-page: 22715 year: 2015 end-page: 22723 ident: bib7 article-title: Recognition of N-glycoforms in human chorionic gonadotropin by monoclonal antibodies and their interaction motifs publication-title: J. Biol. Chem. – volume: 206 year: 2020 ident: bib8 article-title: Development of immobilized enzyme reactors for the characterization of the glycosylation heterogeneity of a protein publication-title: Talanta – volume: 412 start-page: 5729 year: 2020 end-page: 5741 ident: bib11 article-title: Identification and semi-relative quantification of intact glycoforms by nano-LC–(Orbitrap)MS: application to the α-subunit of human chorionic gonadotropin and follicle-stimulating hormone publication-title: Anal. Bioanal. Chem. – reference: Practice Committee of American Society for Reproductive Medicine, Birmingham, Alabama, Gonadotropin preparations: past, present, and future perspectives. Fertil. Steril. 90 (2008) S13-S20. https://doi.org/10.1016/j.fertnstert.2008.08.031 . – volume: 597 start-page: 111 year: 1992 end-page: 122 ident: bib22 article-title: Immobilized lectin columns: useful tools for the fractionation and structural analysis of oligosaccharides publication-title: J. Chromatogr. A – volume: 76 start-page: 134 year: 2016 end-page: 145 ident: bib30 article-title: The molecular relationship between antigenic domains and epitopes on hCG publication-title: Mol. Immunol. – volume: 407 start-page: 1857 year: 2015 end-page: 1869 ident: bib28 article-title: From individual proteins to proteomic samples: characterization of O-glycosylation sites in human chorionic gonadotropin and human-plasma proteins publication-title: Anal. Bioanal. Chem. – volume: 16 start-page: 1207 year: 2006 end-page: 1218 ident: bib2 article-title: Site-specific glycan analysis of human chorionic gonadotropin β-subunit from malignancies and pregnancy by liquid chromatography-electrospray mass spectrometry publication-title: Glycobiology – volume: 23 start-page: 685 year: 2017 end-page: 697 ident: bib18 article-title: Heterogeneous hCG and hMG commercial preparations result in different intracellular signalling but induce a similar long-term progesterone response in vitro publication-title: Mol. Hum. Reprod. – volume: 626 start-page: 356 year: 1980 end-page: 365 ident: bib32 article-title: Affinity titration curves Determination of dissociation constants of lectin-sugar complexes and of their pH-dependence by isoelectric focusing electrophoresis publication-title: BBA - Protein Struct. M. – volume: 193 start-page: 77 year: 2019 end-page: 86 ident: bib14 article-title: First characterizations by capillary electrophoresis of human chorionic gonadotropin at the intact level publication-title: Talanta – volume: 188 start-page: 271 year: 1990 end-page: 277 ident: bib26 article-title: Lectin affinity chromatography of proteins bearing O-linked oligosaccharides: application of jacalin-agarose publication-title: Anal. Biochem. – volume: 32 start-page: 463 year: 1985 end-page: 472 ident: bib34 article-title: Free alpha subunits of glycoprotein hormone with dissimilar carbohydrates produced by pathologically different carcinomas publication-title: Endocrinol. Jpn. – volume: 1132 start-page: 165 year: 2006 end-page: 173 ident: bib25 article-title: Targeted glycoproteomics: serial lectin affinity chromatography in the selection of O-glycosylation sites on proteins from the human blood proteome publication-title: J. Chromatogr. A – volume: 15 year: 2020 ident: bib9 article-title: Insights into the hyperglycosylation of human chorionic gonadotropin revealed by glycomics analysis publication-title: PLOS One – volume: 81 start-page: 8900 year: 2009 end-page: 8907 ident: bib13 article-title: Profiling the glycoforms of the intact α subunit of recombinant human chorionic gonadotropin by high-resolution capillary electrophoresis-mass spectrometry publication-title: Anal. Chem. – volume: 1640 year: 2021 ident: bib16 article-title: Identification and semi-relative quantification of intact glycoforms of human chorionic gonadotropin alpha and beta subunits by nano liquid chromatography-Orbitrap mass spectrometry publication-title: J. Chromatogr. A – volume: 21 year: 2016 ident: bib23 article-title: Agarose and its derivatives as supports for enzyme immobilization publication-title: Molecules – volume: 36 start-page: S60 year: 2015 end-page: S65 ident: bib1 article-title: Review: hCGs: different sources of production, different glycoforms and functions publication-title: Placenta – volume: 31 start-page: 1121 year: 2014 end-page: 1126 ident: bib21 article-title: Glycan profiling of gestational choriocarcinoma using a lectin microarray publication-title: Oncol. Rep. – volume: 413 start-page: 48 year: 2012 end-page: 65 ident: bib3 article-title: hCG, five independent molecules publication-title: Clin. Chim. Acta – volume: 12 start-page: 23 year: 2018 end-page: 35 ident: bib10 article-title: Analytical characterization of recombinant hCG and comparative studies with reference product publication-title: Biol. Targets Ther. – volume: 10 start-page: 503 year: 2019 ident: bib19 article-title: Glycosylation pattern and in vitro bioactivity of reference follitropin alfa and biosimilars publication-title: Front. Endocrinol. – volume: 16 start-page: 46 year: 2006 end-page: 53 ident: bib24 article-title: Elucidation of binding specificity of Jacalin toward O-glycosylated peptides: quantitative analysis by frontal affinity chromatography publication-title: Glycobiology – volume: 15 start-page: 230 year: 1994 end-page: 235 ident: bib27 article-title: Sugar chain heterogeneity of human urinary chorionic gonadotropin determined by serial lectin affinity chromatography: difference between benign and malignant disease publication-title: Tumor Biol. – volume: 1461 start-page: 84 year: 2016 end-page: 91 ident: bib31 article-title: Development of immobilized-pepsin microreactors coupled to nano liquid chromatography and tandem mass spectrometry for the quantitative analysis of human butyrylcholinesterase publication-title: J. Chromatogr. A – volume: 386 start-page: 133 year: 2009 end-page: 146 ident: bib17 article-title: Specificity analysis of lectins and antibodies using remodeled glycoproteins publication-title: Anal. Biochem. – volume: 242 year: 2024 ident: bib29 article-title: Characterization of Concanavalin A-based lectin-sorbents for the extraction of the human chorionic gonadotropin glycoforms before their analysis by nano liquid chromatography-high resolution mass spectrometry publication-title: J. Pharm. Biomed. Anal. – volume: 178 year: 2020 ident: bib15 article-title: Separation methods hyphenated to mass spectrometry for the characterization of the protein glycosylation at the intact level publication-title: J. Pharm. Biomed. Anal. – volume: 1455 start-page: 315 year: 1999 end-page: 326 ident: bib4 article-title: Structure, pathology and function of the N-linked sugar chains of human chorionic gonadotropin publication-title: Biochim. Biophys. Acta – volume: 122 start-page: 1260 year: 1984 end-page: 1267 ident: bib35 article-title: An oligosaccharide of the O-linked type distinguishes the free from the combined form of hCG alpha subunit publication-title: Biochem. Biophys. Res. Commun. – volume: 412 start-page: 4423 year: 2020 end-page: 4432 ident: bib12 article-title: Analysis of the human chorionic gonadotropin protein at the intact level by HILIC-MS and comparison with RPLC-MS publication-title: Anal. Bioanal. Chem. – volume: 260-262 start-page: 33 year: 2007 end-page: 39 ident: bib20 article-title: Determination of hyperglycosylated human chorionic gonadotropin produced by malignant gestational trophoblastic neoplasias and male germ cell tumors using a lectin-based immunoassay and surface plasmon resonance publication-title: Mol. Cell Endocrinol. – volume: 122 start-page: 1260 year: 1984 ident: 10.1016/j.jpba.2024.116525_bib35 article-title: An oligosaccharide of the O-linked type distinguishes the free from the combined form of hCG alpha subunit publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/0006-291X(84)91228-2 – volume: 178 year: 2020 ident: 10.1016/j.jpba.2024.116525_bib15 article-title: Separation methods hyphenated to mass spectrometry for the characterization of the protein glycosylation at the intact level publication-title: J. Pharm. Biomed. Anal. doi: 10.1016/j.jpba.2019.112921 – volume: 242 year: 2024 ident: 10.1016/j.jpba.2024.116525_bib29 article-title: Characterization of Concanavalin A-based lectin-sorbents for the extraction of the human chorionic gonadotropin glycoforms before their analysis by nano liquid chromatography-high resolution mass spectrometry publication-title: J. Pharm. Biomed. Anal. doi: 10.1016/j.jpba.2024.116022 – volume: 206 year: 2020 ident: 10.1016/j.jpba.2024.116525_bib8 article-title: Development of immobilized enzyme reactors for the characterization of the glycosylation heterogeneity of a protein publication-title: Talanta doi: 10.1016/j.talanta.2019.120171 – volume: 1461 start-page: 84 year: 2016 ident: 10.1016/j.jpba.2024.116525_bib31 article-title: Development of immobilized-pepsin microreactors coupled to nano liquid chromatography and tandem mass spectrometry for the quantitative analysis of human butyrylcholinesterase publication-title: J. Chromatogr. A doi: 10.1016/j.chroma.2016.07.058 – volume: 76 start-page: 134 year: 2016 ident: 10.1016/j.jpba.2024.116525_bib30 article-title: The molecular relationship between antigenic domains and epitopes on hCG publication-title: Mol. Immunol. doi: 10.1016/j.molimm.2016.06.015 – volume: 1526 start-page: 70 year: 2017 ident: 10.1016/j.jpba.2024.116525_bib33 article-title: Development of immunosorbents coupled on-line to immobilized pepsin reactor and micro liquid chromatography–tandem mass spectrometry for analysis of butyrylcholinesterase in human plasma publication-title: J. Chromatogr. A doi: 10.1016/j.chroma.2017.10.033 – volume: 23 start-page: 1 year: 2003 ident: 10.1016/j.jpba.2024.116525_bib5 article-title: Detection of maternal serum hCG glycoform variants in the second trimester of pregnancies affected by down syndrome using a lectin immunoassay publication-title: Prenat. Diagn. doi: 10.1002/pd.507 – volume: 290 start-page: 22715 year: 2015 ident: 10.1016/j.jpba.2024.116525_bib7 article-title: Recognition of N-glycoforms in human chorionic gonadotropin by monoclonal antibodies and their interaction motifs publication-title: J. Biol. Chem. doi: 10.1074/jbc.M115.657072 – volume: 32 start-page: 463 year: 1985 ident: 10.1016/j.jpba.2024.116525_bib34 article-title: Free alpha subunits of glycoprotein hormone with dissimilar carbohydrates produced by pathologically different carcinomas publication-title: Endocrinol. Jpn. doi: 10.1507/endocrj1954.32.463 – volume: 626 start-page: 356 year: 1980 ident: 10.1016/j.jpba.2024.116525_bib32 article-title: Affinity titration curves Determination of dissociation constants of lectin-sugar complexes and of their pH-dependence by isoelectric focusing electrophoresis publication-title: BBA - Protein Struct. M. doi: 10.1016/0005-2795(80)90130-0 – volume: 31 start-page: 1121 year: 2014 ident: 10.1016/j.jpba.2024.116525_bib21 article-title: Glycan profiling of gestational choriocarcinoma using a lectin microarray publication-title: Oncol. Rep. doi: 10.3892/or.2014.2979 – volume: 193 start-page: 77 year: 2019 ident: 10.1016/j.jpba.2024.116525_bib14 article-title: First characterizations by capillary electrophoresis of human chorionic gonadotropin at the intact level publication-title: Talanta doi: 10.1016/j.talanta.2018.09.095 – ident: 10.1016/j.jpba.2024.116525_bib6 doi: 10.1016/j.fertnstert.2008.08.031 – volume: 16 start-page: 46 year: 2006 ident: 10.1016/j.jpba.2024.116525_bib24 article-title: Elucidation of binding specificity of Jacalin toward O-glycosylated peptides: quantitative analysis by frontal affinity chromatography publication-title: Glycobiology doi: 10.1093/glycob/cwj038 – volume: 188 start-page: 271 year: 1990 ident: 10.1016/j.jpba.2024.116525_bib26 article-title: Lectin affinity chromatography of proteins bearing O-linked oligosaccharides: application of jacalin-agarose publication-title: Anal. Biochem. doi: 10.1016/0003-2697(90)90605-9 – volume: 260-262 start-page: 33 year: 2007 ident: 10.1016/j.jpba.2024.116525_bib20 article-title: Determination of hyperglycosylated human chorionic gonadotropin produced by malignant gestational trophoblastic neoplasias and male germ cell tumors using a lectin-based immunoassay and surface plasmon resonance publication-title: Mol. Cell Endocrinol. doi: 10.1016/j.mce.2006.05.010 – volume: 597 start-page: 111 year: 1992 ident: 10.1016/j.jpba.2024.116525_bib22 article-title: Immobilized lectin columns: useful tools for the fractionation and structural analysis of oligosaccharides publication-title: J. Chromatogr. A doi: 10.1016/0021-9673(92)80101-Y – volume: 15 start-page: 230 year: 1994 ident: 10.1016/j.jpba.2024.116525_bib27 article-title: Sugar chain heterogeneity of human urinary chorionic gonadotropin determined by serial lectin affinity chromatography: difference between benign and malignant disease publication-title: Tumor Biol. doi: 10.1159/000217896 – volume: 23 start-page: 685 year: 2017 ident: 10.1016/j.jpba.2024.116525_bib18 article-title: Heterogeneous hCG and hMG commercial preparations result in different intracellular signalling but induce a similar long-term progesterone response in vitro publication-title: Mol. Hum. Reprod. doi: 10.1093/molehr/gax047 – volume: 412 start-page: 4423 year: 2020 ident: 10.1016/j.jpba.2024.116525_bib12 article-title: Analysis of the human chorionic gonadotropin protein at the intact level by HILIC-MS and comparison with RPLC-MS publication-title: Anal. Bioanal. Chem. doi: 10.1007/s00216-020-02684-8 – volume: 1132 start-page: 165 year: 2006 ident: 10.1016/j.jpba.2024.116525_bib25 article-title: Targeted glycoproteomics: serial lectin affinity chromatography in the selection of O-glycosylation sites on proteins from the human blood proteome publication-title: J. Chromatogr. A doi: 10.1016/j.chroma.2006.07.070 – volume: 12 start-page: 23 year: 2018 ident: 10.1016/j.jpba.2024.116525_bib10 article-title: Analytical characterization of recombinant hCG and comparative studies with reference product publication-title: Biol. Targets Ther. doi: 10.2147/BTT.S141203 – volume: 407 start-page: 1857 year: 2015 ident: 10.1016/j.jpba.2024.116525_bib28 article-title: From individual proteins to proteomic samples: characterization of O-glycosylation sites in human chorionic gonadotropin and human-plasma proteins publication-title: Anal. Bioanal. Chem. doi: 10.1007/s00216-014-8439-7 – volume: 1640 year: 2021 ident: 10.1016/j.jpba.2024.116525_bib16 article-title: Identification and semi-relative quantification of intact glycoforms of human chorionic gonadotropin alpha and beta subunits by nano liquid chromatography-Orbitrap mass spectrometry publication-title: J. Chromatogr. A doi: 10.1016/j.chroma.2021.461945 – volume: 21 year: 2016 ident: 10.1016/j.jpba.2024.116525_bib23 article-title: Agarose and its derivatives as supports for enzyme immobilization publication-title: Molecules doi: 10.3390/molecules21111577 – volume: 412 start-page: 5729 year: 2020 ident: 10.1016/j.jpba.2024.116525_bib11 article-title: Identification and semi-relative quantification of intact glycoforms by nano-LC–(Orbitrap)MS: application to the α-subunit of human chorionic gonadotropin and follicle-stimulating hormone publication-title: Anal. Bioanal. Chem. doi: 10.1007/s00216-020-02794-3 – volume: 413 start-page: 48 year: 2012 ident: 10.1016/j.jpba.2024.116525_bib3 article-title: hCG, five independent molecules publication-title: Clin. Chim. Acta doi: 10.1016/j.cca.2011.09.037 – volume: 10 start-page: 503 year: 2019 ident: 10.1016/j.jpba.2024.116525_bib19 article-title: Glycosylation pattern and in vitro bioactivity of reference follitropin alfa and biosimilars publication-title: Front. Endocrinol. doi: 10.3389/fendo.2019.00503 – volume: 81 start-page: 8900 year: 2009 ident: 10.1016/j.jpba.2024.116525_bib13 article-title: Profiling the glycoforms of the intact α subunit of recombinant human chorionic gonadotropin by high-resolution capillary electrophoresis-mass spectrometry publication-title: Anal. Chem. doi: 10.1021/ac901506p – volume: 386 start-page: 133 year: 2009 ident: 10.1016/j.jpba.2024.116525_bib17 article-title: Specificity analysis of lectins and antibodies using remodeled glycoproteins publication-title: Anal. Biochem. doi: 10.1016/j.ab.2008.12.005 – volume: 15 year: 2020 ident: 10.1016/j.jpba.2024.116525_bib9 article-title: Insights into the hyperglycosylation of human chorionic gonadotropin revealed by glycomics analysis publication-title: PLOS One doi: 10.1371/journal.pone.0228507 – volume: 16 start-page: 1207 year: 2006 ident: 10.1016/j.jpba.2024.116525_bib2 article-title: Site-specific glycan analysis of human chorionic gonadotropin β-subunit from malignancies and pregnancy by liquid chromatography-electrospray mass spectrometry publication-title: Glycobiology doi: 10.1093/glycob/cwl034 – volume: 36 start-page: S60 year: 2015 ident: 10.1016/j.jpba.2024.116525_bib1 article-title: Review: hCGs: different sources of production, different glycoforms and functions publication-title: Placenta doi: 10.1016/j.placenta.2015.02.002 – volume: 1455 start-page: 315 year: 1999 ident: 10.1016/j.jpba.2024.116525_bib4 article-title: Structure, pathology and function of the N-linked sugar chains of human chorionic gonadotropin publication-title: Biochim. 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| Title | Evaluation of Jacalin lectin sorbents for the extraction of the human chorionic gonadotropin glycoforms prior to analysis by nano liquid chromatography-high resolution mass spectrometry |
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