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Title:Disulfide Cross -Linking in Protein Microspheres
Author(s):Szewczyk, Gregory W.
Doctoral Committee Chair(s):Kenneth S. Suslick
Department / Program:Chemistry
Discipline:Chemistry
Degree Granting Institution:University of Illinois at Urbana-Champaign
Degree:Ph.D.
Genre:Dissertation
Subject(s):Chemistry, Inorganic
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.
Issue Date:2000
Type:Text
Language:English
Description:208 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2000.
URI:http://hdl.handle.net/2142/84500
Other Identifier(s):(MiAaPQ)AAI9990154
Date Available in IDEALS:2015-09-25
Date Deposited:2000


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