Proteome Analysis by Three-Dimensional Protein Separation: Turnover of Cytosolic Proteins in Hepatocytes
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Stefan Stevanovic
and Peter Bohley
Abstract
We performed a threedimensional separation of pulsechase duallabelled rat liver cytosolic proteins using hydrophobic interaction chromatography, isoelectric focusing, and SDS gel electrophoresis. Due to very different expression rates but similar size and pI of rat liver cytosolic proteins, we demonstrate the impossibility of successful twodimensional separations of such complex protein mixtures. A prefractionation of proteins by hydrophobic interaction chromatography is therefore recommended prior to twodimensional gel electrophoresis. Our studies confirmed the correlation between protein turnover rates and surface hydrophobicity.
Copyright © 2001 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
- Vaccine Development: from Empirical Medicine to Molecularly Designed Therapy
- Dendritic Cells for Specific Cancer Immunotherapy
- Intracellular Bacteria as Targets and Carriers for Vaccination
- Bacteria-Mediated Transfer of Eukaryotic Expression Plasmids into Mammalian Host Cells
- Revealing the Potential of DNA-Based Vaccination: Lessons Learned from the Hepatitis B Virus Surface Antigen
- Progress toward a Malaria Vaccine: Efficient Induction of Protective Anti-Malaria Immunity
- Peptide Vaccines and Peptide Libraries
- Defined Synthetic Vaccines
- Antimicrobial Peptides: Properties and Applicability
- G-Quadruplex DNA Structures Variations on a Theme
- The Role of Heat Shock Proteins and Their Receptors in the Activation of the Immune System
- Transcriptional Repression Mediated by the KRAB Domain of the Human C2H2 Zinc Finger Protein Kox1/ZNF10 Does Not Require Histone Deacetylation
- Structure and Evolution of 4-Coumarate:Coenzyme A Ligase (4CL) Gene Families
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