{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,3,22]],"date-time":"2025-03-22T12:36:13Z","timestamp":1742646973424,"version":"3.37.3"},"reference-count":35,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,10,23]],"date-time":"2025-10-23T00:00:00Z","timestamp":1761177600000},"content-version":"am","delay-in-days":295,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,1,1]],"date-time":"2025-01-01T00:00:00Z","timestamp":1735689600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100007601","name":"Horizon 2020","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100007601","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010661","name":"Horizon 2020 Framework Programme","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100010661","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010665","name":"H2020 Marie Sk\u0142odowska-Curie Actions","doi-asserted-by":"publisher","award":["754387"],"award-info":[{"award-number":["754387"]}],"id":[{"id":"10.13039\/100010665","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Pharmaceutical and Biomedical Analysis"],"published-print":{"date-parts":[[2025,1]]},"DOI":"10.1016\/j.jpba.2024.116525","type":"journal-article","created":{"date-parts":[[2024,10,15]],"date-time":"2024-10-15T15:18:30Z","timestamp":1729005510000},"page":"116525","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"special_numbering":"C","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"],"prefix":"10.1016","volume":"252","author":[{"given":"Anastasia","family":"Goumenou","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christophe","family":"Chendo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Audrey","family":"Comb\u00e8s","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Thierry","family":"Fournier","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Val\u00e9rie","family":"Pichon","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nathalie","family":"Delaunay","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.jpba.2024.116525_bib1","doi-asserted-by":"crossref","first-page":"S60","DOI":"10.1016\/j.placenta.2015.02.002","article-title":"Review: hCGs: different sources of production, different glycoforms and functions","volume":"36","author":"Fournier","year":"2015","journal-title":"Placenta"},{"key":"10.1016\/j.jpba.2024.116525_bib2","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1093\/glycob\/cwl034","article-title":"Site-specific glycan analysis of human chorionic gonadotropin \u03b2-subunit from malignancies and pregnancy by liquid chromatography-electrospray mass spectrometry","volume":"16","author":"Valmu","year":"2006","journal-title":"Glycobiology"},{"key":"10.1016\/j.jpba.2024.116525_bib3","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.cca.2011.09.037","article-title":"hCG, five independent molecules","volume":"413","author":"Cole","year":"2012","journal-title":"Clin. Chim. Acta"},{"key":"10.1016\/j.jpba.2024.116525_bib4","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1016\/S0925-4439(99)00060-5","article-title":"Structure, pathology and function of the N-linked sugar chains of human chorionic gonadotropin","volume":"1455","author":"Kobata","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jpba.2024.116525_bib5","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/pd.507","article-title":"Detection of maternal serum hCG glycoform variants in the second trimester of pregnancies affected by down syndrome using a lectin immunoassay","volume":"23","author":"Talbot","year":"2003","journal-title":"Prenat. Diagn."},{"key":"10.1016\/j.jpba.2024.116525_bib6","doi-asserted-by":"crossref","unstructured":"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 .","DOI":"10.1016\/j.fertnstert.2008.08.031"},{"key":"10.1016\/j.jpba.2024.116525_bib7","doi-asserted-by":"crossref","first-page":"22715","DOI":"10.1074\/jbc.M115.657072","article-title":"Recognition of N-glycoforms in human chorionic gonadotropin by monoclonal antibodies and their interaction motifs","volume":"290","author":"Li","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jpba.2024.116525_bib8","doi-asserted-by":"crossref","DOI":"10.1016\/j.talanta.2019.120171","article-title":"Development of immobilized enzyme reactors for the characterization of the glycosylation heterogeneity of a protein","volume":"206","author":"Perchepied","year":"2020","journal-title":"Talanta"},{"key":"10.1016\/j.jpba.2024.116525_bib9","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0228507","article-title":"Insights into the hyperglycosylation of human chorionic gonadotropin revealed by glycomics analysis","volume":"15","author":"Ibeto","year":"2020","journal-title":"PLOS One"},{"key":"10.1016\/j.jpba.2024.116525_bib10","doi-asserted-by":"crossref","first-page":"23","DOI":"10.2147\/BTT.S141203","article-title":"Analytical characterization of recombinant hCG and comparative studies with reference product","volume":"12","author":"Thennati","year":"2018","journal-title":"Biol. Targets Ther."},{"key":"10.1016\/j.jpba.2024.116525_bib11","doi-asserted-by":"crossref","first-page":"5729","DOI":"10.1007\/s00216-020-02794-3","article-title":"Identification and semi-relative quantification of intact glycoforms by nano-LC\u2013(Orbitrap)MS: application to the \u03b1-subunit of human chorionic gonadotropin and follicle-stimulating hormone","volume":"412","author":"Al Matari","year":"2020","journal-title":"Anal. Bioanal. Chem."},{"key":"10.1016\/j.jpba.2024.116525_bib12","doi-asserted-by":"crossref","first-page":"4423","DOI":"10.1007\/s00216-020-02684-8","article-title":"Analysis of the human chorionic gonadotropin protein at the intact level by HILIC-MS and comparison with RPLC-MS","volume":"412","author":"Camperi","year":"2020","journal-title":"Anal. Bioanal. Chem."},{"key":"10.1016\/j.jpba.2024.116525_bib13","doi-asserted-by":"crossref","first-page":"8900","DOI":"10.1021\/ac901506p","article-title":"Profiling the glycoforms of the intact \u03b1 subunit of recombinant human chorionic gonadotropin by high-resolution capillary electrophoresis-mass spectrometry","volume":"81","author":"Thakur","year":"2009","journal-title":"Anal. Chem."},{"key":"10.1016\/j.jpba.2024.116525_bib14","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.talanta.2018.09.095","article-title":"First characterizations by capillary electrophoresis of human chorionic gonadotropin at the intact level","volume":"193","author":"Camperi","year":"2019","journal-title":"Talanta"},{"key":"10.1016\/j.jpba.2024.116525_bib15","doi-asserted-by":"crossref","DOI":"10.1016\/j.jpba.2019.112921","article-title":"Separation methods hyphenated to mass spectrometry for the characterization of the protein glycosylation at the intact level","volume":"178","author":"Camperi","year":"2020","journal-title":"J. Pharm. Biomed. Anal."},{"key":"10.1016\/j.jpba.2024.116525_bib16","doi-asserted-by":"crossref","DOI":"10.1016\/j.chroma.2021.461945","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","volume":"1640","author":"Al Matari","year":"2021","journal-title":"J. Chromatogr. A"},{"key":"10.1016\/j.jpba.2024.116525_bib17","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.ab.2008.12.005","article-title":"Specificity analysis of lectins and antibodies using remodeled glycoproteins","volume":"386","author":"Iskratsch","year":"2009","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.jpba.2024.116525_bib18","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1093\/molehr\/gax047","article-title":"Heterogeneous hCG and hMG commercial preparations result in different intracellular signalling but induce a similar long-term progesterone response in vitro","volume":"23","author":"Riccetti","year":"2017","journal-title":"Mol. Hum. Reprod."},{"key":"10.1016\/j.jpba.2024.116525_bib19","doi-asserted-by":"crossref","first-page":"503","DOI":"10.3389\/fendo.2019.00503","article-title":"Glycosylation pattern and in vitro bioactivity of reference follitropin alfa and biosimilars","volume":"10","author":"Riccetti","year":"2019","journal-title":"Front. Endocrinol."},{"key":"10.1016\/j.jpba.2024.116525_bib20","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.mce.2006.05.010","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","volume":"260-262","author":"Kelly","year":"2007","journal-title":"Mol. Cell Endocrinol."},{"key":"10.1016\/j.jpba.2024.116525_bib21","doi-asserted-by":"crossref","first-page":"1121","DOI":"10.3892\/or.2014.2979","article-title":"Glycan profiling of gestational choriocarcinoma using a lectin microarray","volume":"31","author":"Kobayashi","year":"2014","journal-title":"Oncol. Rep."},{"key":"10.1016\/j.jpba.2024.116525_bib22","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/0021-9673(92)80101-Y","article-title":"Immobilized lectin columns: useful tools for the fractionation and structural analysis of oligosaccharides","volume":"597","author":"Kobata","year":"1992","journal-title":"J. Chromatogr. A"},{"key":"10.1016\/j.jpba.2024.116525_bib23","doi-asserted-by":"crossref","DOI":"10.3390\/molecules21111577","article-title":"Agarose and its derivatives as supports for enzyme immobilization","volume":"21","author":"Zucca","year":"2016","journal-title":"Molecules"},{"key":"10.1016\/j.jpba.2024.116525_bib24","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1093\/glycob\/cwj038","article-title":"Elucidation of binding specificity of Jacalin toward O-glycosylated peptides: quantitative analysis by frontal affinity chromatography","volume":"16","author":"Tachibana","year":"2006","journal-title":"Glycobiology"},{"key":"10.1016\/j.jpba.2024.116525_bib25","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.chroma.2006.07.070","article-title":"Targeted glycoproteomics: serial lectin affinity chromatography in the selection of O-glycosylation sites on proteins from the human blood proteome","volume":"1132","author":"Durham","year":"2006","journal-title":"J. Chromatogr. A"},{"key":"10.1016\/j.jpba.2024.116525_bib26","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/0003-2697(90)90605-9","article-title":"Lectin affinity chromatography of proteins bearing O-linked oligosaccharides: application of jacalin-agarose","volume":"188","author":"Hortin","year":"1990","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.jpba.2024.116525_bib27","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1159\/000217896","article-title":"Sugar chain heterogeneity of human urinary chorionic gonadotropin determined by serial lectin affinity chromatography: difference between benign and malignant disease","volume":"15","author":"Sakai","year":"1994","journal-title":"Tumor Biol."},{"key":"10.1016\/j.jpba.2024.116525_bib28","doi-asserted-by":"crossref","first-page":"1857","DOI":"10.1007\/s00216-014-8439-7","article-title":"From individual proteins to proteomic samples: characterization of O-glycosylation sites in human chorionic gonadotropin and human-plasma proteins","volume":"407","author":"Bai","year":"2015","journal-title":"Anal. Bioanal. Chem."},{"key":"10.1016\/j.jpba.2024.116525_bib29","doi-asserted-by":"crossref","DOI":"10.1016\/j.jpba.2024.116022","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","volume":"242","author":"Goumenou","year":"2024","journal-title":"J. Pharm. Biomed. Anal."},{"key":"10.1016\/j.jpba.2024.116525_bib30","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.molimm.2016.06.015","article-title":"The molecular relationship between antigenic domains and epitopes on hCG","volume":"76","author":"Berger","year":"2016","journal-title":"Mol. Immunol."},{"key":"10.1016\/j.jpba.2024.116525_bib31","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.chroma.2016.07.058","article-title":"Development of immobilized-pepsin microreactors coupled to nano liquid chromatography and tandem mass spectrometry for the quantitative analysis of human butyrylcholinesterase","volume":"1461","author":"Bonichon","year":"2016","journal-title":"J. Chromatogr. A"},{"key":"10.1016\/j.jpba.2024.116525_bib32","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1016\/0005-2795(80)90130-0","article-title":"Affinity titration curves Determination of dissociation constants of lectin-sugar complexes and of their pH-dependence by isoelectric focusing electrophoresis","volume":"626","author":"Ek","year":"1980","journal-title":"BBA - Protein Struct. M."},{"key":"10.1016\/j.jpba.2024.116525_bib33","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.chroma.2017.10.033","article-title":"Development of immunosorbents coupled on-line to immobilized pepsin reactor and micro liquid chromatography\u2013tandem mass spectrometry for analysis of butyrylcholinesterase in human plasma","volume":"1526","author":"Bonichon","year":"2017","journal-title":"J. Chromatogr. A"},{"key":"10.1016\/j.jpba.2024.116525_bib34","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1507\/endocrj1954.32.463","article-title":"Free alpha subunits of glycoprotein hormone with dissimilar carbohydrates produced by pathologically different carcinomas","volume":"32","author":"Nishimura","year":"1985","journal-title":"Endocrinol. Jpn."},{"key":"10.1016\/j.jpba.2024.116525_bib35","doi-asserted-by":"crossref","first-page":"1260","DOI":"10.1016\/0006-291X(84)91228-2","article-title":"An oligosaccharide of the O-linked type distinguishes the free from the combined form of hCG alpha subunit","volume":"122","author":"Cole","year":"1984","journal-title":"Biochem. Biophys. Res. Commun."}],"container-title":["Journal of Pharmaceutical and Biomedical Analysis"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0731708524005673?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0731708524005673?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,11,3]],"date-time":"2024-11-03T19:27:44Z","timestamp":1730662064000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0731708524005673"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,1]]},"references-count":35,"alternative-id":["S0731708524005673"],"URL":"https:\/\/doi.org\/10.1016\/j.jpba.2024.116525","relation":{},"ISSN":["0731-7085"],"issn-type":[{"type":"print","value":"0731-7085"}],"subject":[],"published":{"date-parts":[[2025,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"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","name":"articletitle","label":"Article Title"},{"value":"Journal of Pharmaceutical and Biomedical Analysis","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jpba.2024.116525","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 Elsevier B.V. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"116525"}}