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  • 1985-1989  (4)
  • Analytical Chemistry and Spectroscopy  (2)
  • Carcinoma of the uterus  (1)
  • Proteolysis  (1)
Source
Material
Years
Year
Keywords
  • 1
    Electronic Resource
    Electronic Resource
    Immunolocalization of cathepsins B, H and L in skeletal muscle of X-linked muscular dystrophy (mdx) mouse (1988)
    Springer
    Acta neuropathologica 75 (1988), S. 217-225 
    Details
    ISSN: 1432-0533
    Keywords: mdx mouse ; Cathepsin L ; Macrophages ; Muscle structural proteins ; Proteolysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The amounts of non-collagen proteins (muscle structural proteins) and the activity of creatine kinase were significantly decreased in muscles of 28-day-old mdx mice. The activities of lysosomal thiol proteases such as cathepsins B and L were increased in muscles of mdx mice at as early as 10 days of age. Endogenous thiol proteinase inhibitor and various lysosomal hydrolases also showed increased activities. The localization of cathepsins B, H and L, and endogenous thiol proteinase inhibitor was investigated using the respective specific antibodies. While only invading macrophages were stained strongly with anticathepsin B and H, and anti-thiol proteinase inhibitor antibodies, cathepsin L was localized in muscle cells as well as in invading macrophages. Cathepsin L in muscle cells itself may initially degrade muscle structural proteins, before lysosomal thiol proteases, mainly derived from macrophages, degrade them in skeletal muscles of mdx mice.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00690529
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Peripheral neuropathy with predominantly motor manifestations in a patient with carcinoma of the uterus (1988)
    Springer
    Journal of neurology 235 (1988), S. 368-370 
    Details
    ISSN: 1432-1459
    Keywords: Motor-dominant neuropathy ; Carcinoma of the uterus ; Paraneoplastic syndrome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary An autopsy case of a 56-year-old woman who had carcinoma of the corpus uteri and peripheral neuropathy with predominantly motor manifestations is described. The neurological abnormalities included subacute weakness of the limbs and loss of deep reflexes, which improved after the surgical removal of the uterine carcinoma. Neuropathologically, peripheral nerves mainly presented features of axonal degeneration with a mild loss of myelinated fibres. Anterior horns of the spinal cord showed central chromatolysis of the motor nerve cells and many spheroids without neuronal loss. Axonopathy of peripheral nerves was considered to be the main pathological process in this paraneoplastic syndrome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00314236
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Structural analysis of protein variants by mass spectrometry: Characterization of haemoglobin providence using a grand-scale mass spectrometer (1989)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 18 (1989), S. 563-565 
    Details
    ISSN: 0887-6134
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A grand-scale mass spectrometer with high mass resolution and high transmission was employed for the analysis of haemoglobin variant. Two variants were isolated from a haemolysate by chromatography. Secondary ion mass spectrometry of complex peptide mixtures derived from these variants precisely determined the molecular weight of abnormal peptides. The molecular weight, 2857.4 and 2858.4, indicated the amino acid substitutions of asparagine and aspartic acid, respectively, for lysine at position 82 of β globin chain. The mutations had been reported in haemoglobin Providence.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200180809
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Application of glycinamidation to the peptide mapping using secondary ion mass spectrometry (1985)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 12 (1985), S. 122-126 
    Details
    ISSN: 1052-9306
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The combined use of glycinamidation with secondary ion mass spectrometry provides a new strategy for the structural analysis of proteins, especially of acidic ones. Elimination of acid residues by glycinamidation facilitated the tryptic digestion of protein, resulting in an improvement in the quality of peptide mapping on mass spectra. The number of acidic amino acid residues in each peptide was easily calculated from the mass increment by glycinamidation without separation of peptides. Further, the glycinamidation makes easier the structural analysis of variant proteins with an acid/amide substitution by augmenting the molecular weight change.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200120306
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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