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2. Redox options in two-dimensional electrophoresis

Author

Manfred Gemeiner, Robin Wait, Francesca Conserva, A. M. Carabelli, Daniela Brambilla, Ingrid Miller, Ivano Eberini, A. Rocco Guerini, R. Ballerio, Shajna Begum, and Elisabetta Gianazza

Subjects
Organic Chemistry, Clinical Biochemistry, Cystine, Proteins, Proteomics, Biochemistry, Redox, Rats, Mice, chemistry.chemical_compound, Electrophoresis, Protein structure, chemistry, Covalent bond, Two dimensional electrophoresis, Settore BIO/10 - Biochimica, Animals, Humans, Cattle, Electrophoresis, Gel, Two-Dimensional, Isoelectric Focusing, Oxidation-Reduction, Cysteine
Abstract

Two-dimensional electrophoresis is usually run on fully reduced samples. Under these conditions even covalently bound oligomers are dissociated and individual polypeptide chains may be fully unfolded by both, urea and SDS, which maximizes the number of resolved components and allows their pI and M(r) to be most accurately evaluated. However, various electrophoretic protocols for protein structure investigation require a combination of steps under varying redox conditions. We review here some of the applications of these procedures. We also present some original data about a few related samples -- serum from four species: Homo sapiens, Mus musculus, Rattus norvegicus, Bos taurus -- which we run under fully unreduced and fully reduced conditions as well as with reduction between first and second dimension. We demonstrate that in many cases the unreduced proteins migrate with a better resolution than reduced proteins, mostly in the crowded 'alpha-globulin' area of pI 4.5-6 and M(r) 50-70 kDa.

Published
2005
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3. Redox options in two-dimensional electrophoresis.

Author

R. Wait, S. Begum, D. Brambilla, A. M. Carabelli, F. Conserva, A. Rocco Guerini, I. Eberini, R. Ballerio, M. Gemeiner, I. Miller, and E. Gianazza

Abstract

Summary. Two-dimensional electrophoresis is usually run on fully reduced samples. Under these conditions even covalently bound oligomers are dissociated and individual polypeptide chains may be fully unfolded by both, urea and SDS, which maximizes the number of resolved components and allows their pI and Mr to be most accurately evaluated. However, various electrophoretic protocols for protein structure investigation require a combination of steps under varying redox conditions. We review here some of the applications of these procedures. We also present some original data about a few related samples – serum from four species: Homo sapiens, Mus musculus, Rattus norvegicus, Bos taurus – which we run under fully unreduced and fully reduced conditions as well as with reduction between first and second dimension. We demonstrate that in many cases the unreduced proteins migrate with a better resolution than reduced proteins, mostly in the crowded ‘a-globulin’ area of pI 4.5–6 and Mr 50–70?kDa. [ABSTRACT FROM AUTHOR]

Published
2005

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