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https://hdl.handle.net/2142/84500
Description
Title
Disulfide Cross -Linking in Protein Microspheres
Author(s)
Szewczyk, Gregory W.
Issue Date
2000
Doctoral Committee Chair(s)
Kenneth S. Suslick
Department of Study
Chemistry
Discipline
Chemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Chemistry, Inorganic
Language
eng
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.
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