Disulfide Cross -Linking in Protein Microspheres

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.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Chemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Szewczyk, Gregory W.

Contributors dc:contributor

• Kenneth S. Suslick

• Chemistry, Inorganic

Language dc:language

eng

Identifier

(MiAaPQ)AAI9990154

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/84500