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  • 1
    ISSN: 1432-2307
    Keywords: Atrial natriuretic peptide ; Conduction system ; Cardiac disease ; Immunohistochemistry ; Northern blotting
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Atrial natriuretic peptide (ANP), a cardiac hormone, is known to be located in the atrial specific granules, but its presence and localization in the ventricular muscle of the human heart has not been examined fully. Using a specific antibody to human ANP, we studied the conduction system and ventricular muscle with immunohistochemical and ultrastructural methods in 30 hearts obtained at autopsy. These included 12 normal and 18 diseased hearts. In the normal hearts, ANP-positive granules, which were regularly observed in the atrial myocytes, were found in small quantities in the cells of the penetrating and branching bundles in 4 of 12, and in the cells of the ventricular free walls in 2 of the 12 hearts. In the diseased hearts, the positivity increased significantly (P〈0.05), being found in 13 of 18 (72.2%) conduction systems and 10 of 18 (55.6%) ventricular muscles. The granules were confirmed to be immunoreactive with ANP by ultrastructural examination. Furthermore, the presence of ANP mRNA in the conduction system as well as in the ventricular myocytes was demonstrated by Northern blot hybridization for which we used the complementary DNA of human ANP. Thus, a small quantity of ANP appears to be synthesized and stored in the conduction system and ventricles of some normal hearts. However, ANP was shown to be present in a larger percentage of the diseased hearts.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Chichester [u.a.] : Wiley-Blackwell
    Journal of Raman Spectroscopy 18 (1987), S. 119-122 
    ISSN: 0377-0486
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Raman spectra of yeast alcohol dehydrogenase in buffered, aqueous solutions and in D2O, and FTIR spectra of aqueous solutions and thin films have been collected and analyzed. No significant differences between the Raman spectra in the pH range 6.00-7.50 and between the infrared spectra of the solution and film have been observed. The tyrosine doublet strongly favors exposed hydroxyl groups and the Raman spectra indicate multiple conformations for the disulfide moieties. Analysis of Raman intensities favors significant α-helix and random coil contents. The secondary structure of yeast alcohol dehydrogenase based on Raman data is compared with the better characterized secondary structure of equine liver alcohol dehydrogenase.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Chichester [u.a.] : Wiley-Blackwell
    Journal of Raman Spectroscopy 19 (1988), S. 267-269 
    ISSN: 0377-0486
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Raman spectra of porcine mitochondrial malate dehydrogenase have been collected and analysed. The existence of weak hydrogen bonds is indicated by the intensity ratio of the tyrosine doublet and a band is found which can be attributed to disulfide bonds. The observed frequencies in the amide I and III regions favor significant contributions from α-helix and random conformations. An analysis of the intensities using standard methods predicts a very low β-sheet content.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
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