{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["11(4)"],"submitter":["Robotham AC"],"pubmed_abstract":["The detection of free sulfhydryls in proteins can reveal incomplete disulfide bond formation, indicate cysteine residues available for conjugation, and offer insights into protein stability and structure. Traditional spectroscopic methods of free sulfhydryl detection, such as Ellman's reagent, generally require a relatively large amount of sample, preventing their use for the analysis of biotherapeutics early in the development cycle. These spectroscopic methods also cannot accurately determine the location of the free sulfhydryl, further limiting their utility. Mass spectrometry was used to detect free sulfhydryl residues in intact proteins after labeling with Maleimide-PEG<sub>2</sub>-Biotin. As little as 2% cysteine residues with free sulfhydryls (0.02 mol SH per mol protein) could be d"],"journal":["mAbs"],"pagination":["757-766"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6601545"],"repository":["biostudies-literature"],"pubmed_title":["Detection and quantification of free sulfhydryls in monoclonal antibodies using maleimide labeling and mass spectrometry."],"pmcid":["PMC6601545"],"pubmed_authors":["Robotham AC","Kelly JF"],"additional_accession":[]},"is_claimable":false,"name":"Detection and quantification of free sulfhydryls in monoclonal antibodies using maleimide labeling and mass spectrometry.","description":"The detection of free sulfhydryls in proteins can reveal incomplete disulfide bond formation, indicate cysteine residues available for conjugation, and offer insights into protein stability and structure. Traditional spectroscopic methods of free sulfhydryl detection, such as Ellman's reagent, generally require a relatively large amount of sample, preventing their use for the analysis of biotherapeutics early in the development cycle. These spectroscopic methods also cannot accurately determine the location of the free sulfhydryl, further limiting their utility. Mass spectrometry was used to detect free sulfhydryl residues in intact proteins after labeling with Maleimide-PEG<sub>2</sub>-Biotin. As little as 2% cysteine residues with free sulfhydryls (0.02 mol SH per mol protein) could be d","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 May/Jun","modification":"2025-04-22T20:27:25.979Z","creation":"2019-07-25T07:01:13Z"},"accession":"S-EPMC6601545","cross_references":{"pubmed":["30894096"],"doi":["10.1080/19420862.2019.1595307"]}}