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  • 1
    Electronic Resource
    Electronic Resource
    Qualitative and quantitative variability in different classes of proteins: Comparison of mouse and rat (1987)
    Springer
    Journal of molecular evolution 24 (1987), S. 260-271 
    Details
    ISSN: 1432-1432
    Keywords: Mouse ; Rat ; Two-dimensional electrophoresis ; Quantitative variability of proteins ; Qualitative variability of proteins ; Protein classes ; Membrane proteins ; Organ-specific proteins ; Regulatory genes ; Speciation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Proteins of membranes and cytosols were extracted from the livers and brains of mice (inbred strain DBA/6J) and rats (inbred strain DA/Han) and separated by two-dimensional electrophoresis (2-DE). The 2-DE patterns were compared with regard to qualitative (spot position) and quantitative (spot intensity) characteristics of the proteins of these two species. The following results were obtained: (1) Brain had more (higher percentage) conservative proteins (proteins found in both mice and rats) than liver; (2) plasma membranes had more conservative proteins than the cytosols; (3) organ-unspecific proteins contained more conservative proteins than relatively organ-specific proteins; (4) the pattern of distribution of genetic variability among different classes of proteins represented by findings 1–3 was the same for the qualitative and quantative characteristics of the proteins; and (5) some observations indicated that quantitative variability occurred more frequently among proteins than did qualitative variability. Our conclusion is that regulatory sequences in the DNA (regulatory genes) are subjected to functional constraints that differ in strength among different classes of proteins by the same ratios as the constraints acting on the structural genes. The overall effect of the selective pressure is, however, less stringent for regulatory genes than for structural genes. The results obtained here by comparing two different species are very similar to previous results we obtained by studying different subspecies (inbred strains of the mouse). From this finding arises a new concept: the study of molecular evolution on the basis of different classes of proteins. Our results were compared with data from the literature that were obtained in part from studies on cultured cells. The comparison suggested that cultured cells have lost their tissue-specific proteins, and so generate predominantly extremely conservative proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02111239
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  • 2
    Electronic Resource
    Electronic Resource
    Genetic analysis of the mouse brain proteome (2002)
    [s.l.] : Nature Publishing Group
    Nature genetics 30 (2002), S. 385-393 
    Details
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Proteome analysis is a fundamental step in systematic functional genomics. Here we have resolved 8,767 proteins from the mouse brain proteome by large-gel two-dimensional electrophoresis. We detected 1,324 polymorphic proteins from the European collaborative interspecific backcross. Of these, we ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/ng861
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  • 3
    Electronic Resource
    Electronic Resource
    Analysis of protein patterns from different organs and cell fractions of trisomy 19 mice (1987)
    Springer
    Human genetics 〈Berlin〉 77 (1987), S. 371-378 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Proteins were extracted from liver, brain, and skin of 6-day-old mice with trisomy (Ts) 19 and fractionated into solubilized cell proteins and structure-bound cell proteins. The proteins were separated by two-dimensional electrophoresis, and protein patterns were compared in the combinations Ts/normal and normal/normal. Analysis of the protein patterns revealed protein spots (variants) with densities higher (h-type) or lower (l-type) in trisomies than in normal mice. Some of these variants were found in all Ts individuals investigated for a particular protein class. These variants, termed regular Ts-variants, constituted 0.8%–1.6% of the total number of spots. The proteins of the regular Ts variants were in most cases organ-nonspecific. However, in almost all cases a given quantitative variation was expressed in only one of the three organs investigated. To explain our results, we have presented models for the control of protein levels on the basis of gene regulation. New aspects in the conception of studies on trisomies in man could be gained.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00291429
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  • 4
    Electronic Resource
    Electronic Resource
    Kommutatoren und 2-Cohomologie ϱ-adischer Quaternionenschiefkörper (1986)
    Springer
    Mathematische Zeitschrift 191 (1986), S. 261-282 
    Details
    ISSN: 1432-1823
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01164031
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  • 5
    Electronic Resource
    Electronic Resource
    Metaplektische Erweiterungen von Quaternionenschiefkörpern (1986)
    Springer
    Mathematische Zeitschrift 193 (1986), S. 625-649 
    Details
    ISSN: 1432-1823
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01160480
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  • 6
    Electronic Resource
    Electronic Resource
    Two-dimensional electrophoretic protein patterns of reciprocal hybrids of the mouse strains DBA and C57BL (1992)
    Springer
    Biochemical genetics 30 (1992), S. 649-662 
    Details
    ISSN: 1573-4927
    Keywords: mouse ; reciprocal hybrids ; proteins ; two-dimensional electrophoresis ; genomic imprinting
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Two-dimensional electrophoretic patterns of cytoplasmic liver proteins of the mouse were investigated in reciprocal hybrids of the two inbred mouse strains DBA and C57BL in order to establish whether strain-specific protein variants reveal a mode of inheritance compatible with the concept of genomic imprinting. Variants of this type were found to account for about 11% of approximately 200 variant protein spots scrutinized. Transmission of the maternal form of a variant protein was more frequent than transmission of the paternal form. Maternal/paternal transmission was observed only for proteins showing strain variations in their amount. The results are discussed in terms of the frequency of imprinted genes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02399813
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  • 7
    Electronic Resource
    Electronic Resource
    Composition and genetic variability of heparin-sepharose CL-6B protein fractions obtained from the solubilized proteins of mouse organs (1986)
    Springer
    Biochemical genetics 24 (1986), S. 925-939 
    Details
    ISSN: 1573-4927
    Keywords: protein fractions ; genetic variability ; inbred mice ; heparin-Sepharose chromatography ; two-dimensional electrophoresis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The solubilized proteins of liver and brain from mice of two inbred strains (C57 BL/6J and DBA/2J) and their hybrids were subfractionated by heparin-Sepharose (H-S) CL-6B affinity chromatography. The H-S binding and nonbinding proteins were separated by two-dimensional electrophoresis. The protein patterns obtained were analyzed with regard to their protein composition and their genetic variability (qualitative and quantitative variants). Eighty to ninety percent of the H-S binding proteins were unique to this class of proteins. This class was rich in organ-specific proteins. Compared to the nonbinding proteins the portion of basic proteins was only slightly increased, suggesting that most of the H-S binding proteins interact specifically with heparin. The frequency of qualitative protein variants revealed that H-S binding proteins are more conservative than H-S nonbinding proteins. The quantitative genetic variability was higher in liver than in brain. Quantitative protein variants occurred more frequently than qualitative variants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00554529
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  • 8
    Electronic Resource
    Electronic Resource
    Gel isoelectric focusing of mouse lactate dehydrogenase: Heterogeneity of the isoenzymes A4 and X4 (1975)
    Springer
    Biochemical genetics 13 (1975), S. 707-720 
    Details
    ISSN: 1573-4927
    Keywords: LDH A, B ; LDH X ; isoenzymes ; mouse ; isoelectric focusing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract LDH of mouse organs (including testis) was investigated by isoelectric focusing in polyacrylamide gels. The number of LDH bands in this pattern considerably exceeds the five (six in testis) of the standard electrophoretic pattern. An attempt was made to identify these bands as tetrameric isoenzymes formed by random association of different subunits. This included isoelectric focusing of purified LDH A, B, and X, two-dimensional separation of LDH, urea treatment of LDH, staining with specific substrates, and comparison of different organs. Further experiments were performed to exclude artifacts possibly produced by the isoelectric focusing technique. Different strains of mice were also investigated. The results demonstrate that in addition to the common five LDH bands (A4−B4) one set of five bands is formed by LDH A (A 4 1 −A 4 2 ) and another one by LDH X (X 4 1 −X 4 2 ). Moreover, an unusual band was found which has a lower molecular weight and no affinity to the other isoenzymes. The data suggest that the heterogeneity of the LDH pattern revealed by isoelectric focusing arises from post-transcriptional events rather than from a number of additional genes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00484928
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  • 9
    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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  • 10
    Electronic Resource
    Electronic Resource
    Genetic variability of proteins from mitochondria and mitochondrial fractions of mouse organs (1985)
    Springer
    Biochemical genetics 23 (1985), S. 227-245 
    Details
    ISSN: 1573-4927
    Keywords: protein classes ; genetic variability ; mitochondria ; inbred mice ; two-dimensional electrophoresis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Proteins of whole mitochondria from mouse liver and brain and proteins of liver mitochondrial fractions (plasma and rough membrane fraction) were separated by two-dimensional electrophoresis. Protein patterns of two inbred strains of mouse, C57BL/6J and DBA/2J, and of F1 mice of these two strains were studied. The protein patterns obtained from the different mitochondrial materials were analyzed with regard to their protein composition and the genetic variability of proteins (qualitative and quantitative protein variants). Included in this analysis are data previously obtained from the cytosols and plasma membranes of the same organs and mouse strains. The results showed the following. (1) Mitochondria and organelle-free cell components (cytosol and plasma membranes) have only a few percent of their proteins in common, while two organs, liver and brain, reveal up to approximately 50% organ-nonspecific proteins. The frequency of proteins common to solubilized and structure-bound proteins ranges below 20%. (2) Genetic variability in protein amount occurs much more frequently than genetic variability in protein structure. Liver proteins reveal more genetic variants than brain proteins. Proteins solubilized in the cell show more genetic variation than structure-bound proteins. Furthermore, the results show that with regard to the composition and the genetic variability of proteins, liver and brain differ more in their mitochondria than in their cytosol and plasma membranes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00504321
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