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  • 1
    Electronic Resource
    Electronic Resource
    Genetic variability of proteins from plasma membranes and cytosols of mouse organs (1981)
    Springer
    Biochemical genetics 19 (1981), S. 859-870 
    Details
    ISSN: 1573-4927
    Keywords: genetic variability ; protein amount ; membrane proteins ; inbred mice ; two-dimensional electrophoresis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The genetic variability of membrane proteins (structure-bound proteins) and cytosol proteins (water-soluble proteins) was investigated in two inbred strains of the mouse, C57BL/6J and DBA/2J. Membrane proteins and cytosol were isolated from the brain and liver of the mouse. The proteins were separated by two-dimensional electrophoresis. A high number of genetic variant proteins (brain, 30; liver, 72) was found in the cytosol. Most of these variants represented changes in the amount of proteins. Electrophoretic mobility changes occurred only in about 1% (brain, 6; liver, 9) of all protein spots of a two-dimensional pattern. In contrast to the cytosol proteins, no genetic variation was detected among the membrane proteins, not even for the quantitative characteristics of the protein spots. The results obtained for the two classes of proteins suggest that the degree of variability in the amount of proteins is related to the degree of variability in the structure of proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00504251
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  • 2
    Electronic Resource
    Electronic Resource
    Two-dimensional electrophoresis of membrane and cytosol proteins of mouse liver and brain (1981)
    Weinheim : Wiley-Blackwell
    Electrophoresis 2 (1981), S. 12-24 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Membrane proteins and cytosol proteins from organs (liver, brain) of inbred mice were separated by two-dimensional electrophoresis (2DE). The 2DE technique revealed high resolution of complex protein solutions by staining the proteins. The 2DE patterns of membrane proteins showed about 660 protein spots (polypeptides) for both liver and brain. The protein patterns of the cytosols revealed about 800 polypeptides for the liver and about 680 for the brain. The membrane proteins and cytosol proteins of the 2DE patterns represented two protein populations specific for these two cell components. They matched in 7 % (liver) or 23 % (brain) of the total number of membrane protein spots. The matched spots represented dissociable membrane proteins rather than contamination of the isolated membrane fractions by cytosol proteins. Protein patterns of the same cell fraction but from the two different organs investigated contained more than 50 % organ-unspecific polypeptides.Several conditions of our 2DE standard procedure were reinvestigated to test the usefulness for our technique of some methodical steps employed in 2DE by other authors. We found that many steps often used in sample preparations impaired rather than improved the 2DE pattern. In particular, addition of SDS to the protein sample resulted in a considerable loss of proteins during isoelectric foucing. The 2DE itself could be simplified by omitting several steps such as prefocusing, equilibration of focusing gels, forming gel gradients, autoradiography. This has some implications for the development of 2DE to a routine method.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150020103
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    Paper (German National Licenses)
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