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  • Biochemistry and Biotechnology  (5)
  • 2015-2019
  • 1995-1999  (3)
  • 1990-1994  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Measurement of binding kinetics using the gel electrophoresis mobility shift assay (1993)
    Weinheim : Wiley-Blackwell
    Electrophoresis 14 (1993), S. 725-731 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The gel electrophoresis mobility shift assay is a technique for the qualitative and quantitative analysis of protein-DNA complexes. The ability to resolve reactants, reaction intermediates and products makes this method particularly well-suited for the measurement of the assembly and dissociation rates of protein-nucleic acid complexes. Here we identify conditions that must be met and variations of the technique that are useful for the measurement of reaction rates.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501401115
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  • 2
    Electronic Resource
    Electronic Resource
    Immune complexes in blood: A new strategy for the analysis of their antigen portion (1992)
    Weinheim : Wiley-Blackwell
    Electrophoresis 13 (1992), S. 718-719 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A method is described for the characterization of protein antigens from circulating immune complexes from plasma. Free immunoglobulins G were separated from larger immune complexes by gel filtration with a fast protein liquid chromatographic system. The collected immune complexes were dissociated with 4M urea into antigens and antibodies. With a second column run with 4M urea, antigens smaller than 120 kDa were separated from unloaded antibody fractions. After concentration, they were analyzed by two-dimensional gel electrophoresis.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501301152
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  • 3
    Electronic Resource
    Electronic Resource
    Separation of the two most closely related isoenzymes of alkaline phosphatase by two-dimensional electrophoresis (1995)
    Weinheim : Wiley-Blackwell
    Electrophoresis 16 (1995), S. 1284-1288 
    Details
    ISSN: 0173-0835
    Keywords: Germ cell alkaline phosphatase ; Placental alkaline phosphatase ; Seminoma ; Two-dimensional polyacrylamide gel electrophoresis ; Immobilized pH gradient ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Seminoma is the most frequent testicular germ cell tumor. While effective curative treatment of the disease is available today, there is to date no tumor marker suited for the diagnosis and follow-up. Several authors have suggested that the germ-cell-specific isoenzyme of alkaline phosphatase (GCAP) might be valuable for this purpose. GCAP shows 98% sequence homology with the placental isoenzyme of alkaline phosphatase (PLAP). Both display a high degree of phenotypic heterogeneity. Until now all attempts to raise an antibody reacting specifically with GCAP have failed. Consequently there is no immunological assay that allows the measurement of GCAP in the presence of PLAP. Two-dimensional electrophoresis with a sigmoid immobilized pH-gradient of 3-10 for the first dimension makes it possible to differentiate clearly between these two closely realted isoenzymes. Additionally, it resolves their many phenotypic variants. This is of special interest, since malignant transformation affects the glycosylation patterns of many glycoproteins. For the detection of GCAP and PLAP in two-dimensional electrophoresis it is essential to purify the raw tissue extracts thoroughly. A chromatographic method suited for this purpose is presented.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501601210
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  • 4
    Electronic Resource
    Electronic Resource
    Factors that affect the stability of protein-DNA complexes during gel electrophoresis (1997)
    Weinheim : Wiley-Blackwell
    Electrophoresis 18 (1997), S. 6-11 
    Details
    ISSN: 0173-0835
    Keywords: Complex stability ; Mobility shift assay ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The gel electrophoresis mobility shift assay is widely used for qualitative and quantitative characterization of protein complexes with nucleic acids. Often it is found that complexes persist within electrophoresis gels for much longer than expected on the basis of their free-solution lifetimes. Volume exclusion, direct interaction with gel matrices and the reduction of water activity by the gel have been proposed as mechanisms enhancing the stability of complexes during electrophoresis. We have used the well-characterized interaction of the E. coli cyclic AMP receptor protein (CAP) with lactose promoter DNA to test these proposals. We found that the activity of water within polyacrylamide gels differs little from that of the buffer in which they were cast and that the dependence of the dissociation rate constant on water activity is too small for osmotic stabilization to contribute significantly to the lifetimes of CAP-DNA complexes. In addition, we found that a cross-linked gel matrix is not required for the stabilization of CAP-DNA complexes, that comparable stabilization is produced by three dissimilar polymers (linear polyacrylamide, dextran and polyethylene glycol), and that these polymers stabilize complexes more effectively than equivalent weight concentrations of their cognate monomers. While these results challenge the notion that direct interaction with the gel matrix contributes to the stability of protein-DNA complexes, they are all features expected of excluded volume mechanisms.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150180103
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  • 5
    Electronic Resource
    Electronic Resource
    Electrophoretic analysis of multiple protein-DNA interactions (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 1247-1253 
    Details
    ISSN: 0173-0835
    Keywords: Mobility-shift assay ; Thermodynamics ; Protein-DNA interactions ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Under favorable conditions, native gel electrophoresis allows the resolution of protein-DNA complexes that differ in stoichiometry, identities of occupied DNA sequences (configuration), and macromolecular conformation. This technique provides a unique opportunity to analyze, in thermodynamic terms, the molecular interactions that govern the equilibrium distributions of species in protein-DNA mixtures. Here we describe a general theoretical approach to the analysis of electrophoretic band intensities, and provide examples of its application to the analysis of several interacting systems.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150190804
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