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  • 1990-1994  (2)
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  • 1
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: High resolution two-dimensional electrophoresis (2-DE), using the rat liver as a model, was applied to study hepatocarcinogenesis induced by different chemical carcinogens. Several tumor-associated protein variants were detected by 2-DE in chemically induced rat hepatomas and transformed rat liver cell lines compared to normal rat liver tissue. Proliferation-related protein changes and/or protein alterations due to culture conditions were corrected for by comparison with 2-DE patterns of isolated cells from regenerating liver and short-term cultivated liver cells. Some of the tumor-associated variants were further characterized: (i) By peptide mapping with limited proteolysis we detected clear relationships between several variants. (ii) By studying posttranslational modifications phosphorylated and glycosylated variants could be determined. (iii) A tumor-associated protein variant was identified by amino acid analysis and amino acid sequencing.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Molecular changes occurring in myocardial diseases are not well understood. Proteins, as regulatory molecules, should play an important role in the etiology of these diseases. The method of two-dimensional electrophoresis (2-DE) allows the analysis of some thousand proteins with one experiment. An important prerequisite for this kind of investigation is the possibility of identifying the proteins separated by 2-DE. We resolved 3239 proteins of the human myocardium and tried to identify 33 proteins by amino acid analysis and microsequencing. Twenty proteins were identified by search for the proteinchemical data obtained in the Martinsried Institute Protein Sequence Database. Comparisons of 2-DE patterns of different size, which were obtained in different laboratories, were performed with the result that proteins identified on a 2-DE map of one laboratory can be assigned to spots of 2-DE maps produced by another laboratory. Our results show the usefulness of a myocardial 2-DE database; they can be used in different laboratories and make it possible to generate a collection of important human myocardial proteins in a 2-DE database for comparative studies worldwide.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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