{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/84500"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/84500","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Disulfide Cross -Linking in Protein Microspheres","abstract":"Microspheres composed of either thiol-modified myoglobin or albumin have been extensively examined by a combination of techniques including SDS-PAGE, SEC, and MALDI mass spectrometry peptide mapping. Electrophoresis and chromatography confirm the presence of higher molecular weight protein units as the principle components of the microsphere shell. Treatment with a disulfide reductant established that disulfide bonds are the covalent cross-link between protein molecules. Mass spectrometry has shown that inter-protein disulfide bonding is not random. The disulfide bonds that do form reflect the electrostatic surfaces of the proteins as they approach each other during emulsification and agglomeration.","abstract_html":"Microspheres composed of either thiol-modified myoglobin or albumin have been extensively examined by a combination of techniques including SDS-PAGE, SEC, and MALDI mass spectrometry peptide mapping. Electrophoresis and chromatography confirm the presence of higher molecular weight protein units as the principle components of the microsphere shell. Treatment with a disulfide reductant established that disulfide bonds are the covalent cross-link between protein molecules. Mass spectrometry has shown that inter-protein disulfide bonding is not random. The disulfide bonds that do form reflect the electrostatic surfaces of the proteins as they approach each other during emulsification and agglomeration.","abstract_has_math":false,"creators":["Szewczyk, Gregory W."],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Chemistry","degree_department":null,"school":null,"contributors":["Kenneth S. 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