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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 804 (1996), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 804 (1996), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 804 (1996), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 4
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Journal of Chromatography A 71 (1972), S. 376-379 
    ISSN: 0021-9673
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 386 (1982), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of neurology 202 (1972), S. 331-338 
    ISSN: 1432-1459
    Keywords: Iron Concentration ; Brain Tissue ; Age
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung In 33 Fällen wird die Eisenkonzentration von 13 umschriebenen Regionen des menschlichen Gehirns mittels Atomabsorption ermittelt. Maxima in Höhe von ∼ 800 μg/1 g Trockengewicht zeigen der Globus pallidus, das Putamen und der Nucleus caudatus, Minima von ∼ 100 μg/1 g TG die Oliva inferior und der Balken. Für Frontal- und Occipitalrinde ergibt sich ein Eisengehalt von 200–300 μg/1 g Trockengewicht. Das Verhältnis Eisenkonzentration/Lebensalter ist für die einzelnen untersuchten Regionen z. T. recht unterschiedlich. Während z. B. der Fe-Gehalt in den Basalganglien in den ersten Lebensjahren zunächst sprunghaft, dann jedoch zunehmend flacher ansteigt, ist für die Rindengebiete von Anfang an ein langsames Anwachsen festzustellen. Thalamus und Hippocampus scheinen ihre Fe-Konzentration zeitlebens annähernd konstant zu halten, während in der Olive sogar ein Absinken zu beobachten ist.
    Notes: Summary In 33 autopsy cases the concentration of iron of 13 defined areas of human brain was determined by atomic absorption spectrophotometry. The distribution pattern based on the experimental data shows the highest values of 800 μg/g dry weight in the globus pallidus, putamen and caudate nucleus, the lowest of 100 μg/g dry weight in the oliva inferior and corpus callosum, with intermediate values of 200 to 300 μg/g dry weight in the frontal and occipital cortex. The iron content in relation to age was found to differ (considerably) among the various brain areas examined. There is a sharp rise in iron content of the basal ganglia during the first years of life followed by a gradual levelling off. The increase in iron content of cerebral cortex was observed to be much less marked. Both thalamus and hippocampus show little change in their iron content (during life), while the olives have a tendency to lose iron.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Virchows Archiv 354 (1971), S. 268-284 
    ISSN: 1432-2307
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Gewebe eines an einer spontanen Ruptur der Nierenarterie verstorbenen Mannes mit den klinischen Zeichen eines Ehlers-Danlos-Syndroms wurde morphologisch und chemisch untersucht. Als Ursache für das auffällige Verhalten der EDS-Gewebe wird ein Fehlverhalten des Elastin angesehen. Dieses beruht auf einer verminderten Zugfestigkeit und einer schlechten bzw. gestörten Verankerung elastischer Lamellen im Gewebe. Eine Störung der Biosynthese von Desmosinen wird für die verminderte Zugfestigkeit von Elastin verantwortlich gemacht und ist in einem erhöhten Lysingehalt widergespiegelt. Die schlechte Verankerung elastischer Lamellen im Gewebe wird auf das Fehlen eines peripheren Besatzes aus Mikrofibrillen zurückgeführt. Das Kollagen liegt im EDS-Gewebe relativ oft im gequollenen Zustand vor und kann deshalb funktionell ebenfalls ein Fehlverhalten zeigen. Auf die Möglichkeit einer Verwechslung von gequollenem Kollagen und Elastin wird hingewiesen.
    Notes: Summary Results are reported of morphological and chemical studies of various tissues of a patient with the clinical signs of an Ehlers-Danlos syndrome (EDS) who died from a spontaneous rupture of the renal artery. It is assumed that the cause for the remarkable properties of the tissues of EDS lies in a disorder of the elastin. This is caused by a diminished strenght and a poor, and abnormal linkage of the elastic lamellae in tissue. A disturbed biosynthesis of desmosins is made responsible for the diminished strength and is reflected by an increased content in lysin. The impaired linkage of the elastic lamellae is the result of an absent microfibrillar border. The collagen fibers are often swollen and therefore may be functionally impaired. The possibility of mistaking swollen collagen for elastin is discussed.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Histochemistry and cell biology 106 (1996), S. 105-114 
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The immunogold labeling technique has been extremely useful in investigation of the structure and function of peroxisomes. In this report a few examples of the application of this technique with significant implications in the field are briefly reviewd. The problem of extra-peroxisomal catalase, the subject of long controversy between the biochemists and cytochemists, was settled with the immunogold technique, which unequivocally revealed the presence of that enzyme not only in the cytoplasm, but also in the euchromatin region of nucleus, in addition to peroxisomes. On the other hand, lactate dehydrogenase, a typical cytoplasmic protein, has also been shown recently to be present in peroxisomes and to be involved in the reoxidation of NADH produced by the peroxisomal β-oxidation system. The immunogold technique has revealed several distinct compartments in the matrix of mammalian peroxisomes: urate oxidase in the crystalline cores, α-hydroxy acid oxidase B in the marginal plates andd-amino acid oxidase in a non-crystaline condensed region of matrix. The specific alterations of peroxisomal proteins are reflected in their immunolabeling density with gold particles. Quantitation of gold-label by automatic image analysis has revealed that the induction of lipid β-oxidation enzyme proteins by diverse hypolipidemic drugs is initiated and more pronounced in the pericentral region of the liver lobule. Finally, immunogold labeling with an antibody to 70 kDa peroxisomal membrane protein has identified a novel class of small peroxisomes that initially incorporate radioactive amino acids more efficiently than regular peroxisomes and thus may represent early stages in the biogenesis of peroxisomes.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Histochemistry and cell biology 106 (1996), S. 105-114 
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  The immunogold labeling technique has been extremely useful in investigation of the structure and function of peroxisomes. In this report a few examples of the application of this technique with significant implications in the field are briefly reviewed. The problem of extraperoxisomal catalase, the subject of long controversy between the biochemists and cytochemists, was settled with the immunogold technique, which unequivocally revealed the presence of that enzyme not only in the cytoplasm, but also in the euchromatin region of nucleus, in addition to peroxisomes. On the other hand, lactate dehydrogenase, a typical cytoplasmic protein, has also been shown recently to be present in peroxisomes and to be involved in the reoxidation of NADH produced by the peroxisomal β-oxidation system. The immunogold technique has revealed several distinct compartments in the matrix of mammalian peroxisomes: urate oxidase in the crystalline cores, α-hydroxy acid oxidase B in the marginal plates and d-amino acid oxidase in a non-crystaline condensed region of matrix. The specific alterations of peroxisomal proteins are reflected in their immunolabeling density with gold particles. Quantitation of gold-label by automatic image analysis has revealed that the induction of lipid β-oxidation enzyme proteins by diverse hypolipidemic drugs is initiated and more pronounced in the pericentral region of the liver lobule. Finally, immunogold labeling with an antibody to 70 kDa peroxisomal membrane protein has identified a novel class of small peroxisomes that initially incorporate radioactive amino acids more efficiently than regular peroxisomes and thus may represent early stages in the biogenesis of peroxisomes.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Peroxisomes of the digestive glands of mussels, Mytilus galloprovincialis Lmk, were investigated by immunoblotting and immunohistochemistry using rabbit antibodies against several mammalian hepatic peroxisomal proteins. Western blot analysis of main subcellular fractions revealed immunoreactive polypeptides with molecular weights comparable to those of the corresponding mammalian hepatic proteins. They could be localized to the peroxisomal matrix in the case of catalase, multifunctional enzyme (PH), and palmitoyl-CoA oxidase (AOX), and to the peroxisomal membrane in respect to PMP 70. The purification of peroxisomes by metrizamide density gradient centrifugation revealed the existence of two subpopulations with densities of 1.16 and 1.20 g cm–3 exhibiting different protein compositions. In paraffin sections, positive immunolabeling for catalase was distributed along the apical cytoplasm of the epithelia of digestive ducts and stomach and throughout the cytoplasm of digestive tubule cells. The peroxisomal β-oxidation enzymes, AOX and PH, also appeared predominantly in the ducts and the stomach epithelia with a weaker immunolabeling in the tubules. At the electron microscopic level a clear labeling with gold particles was observed in the peroxisomal matrix with the anti-guinea pig catalase antibody. In addition to peroxisomes, the anti-PH antibody also labeled the mitochondria. The similarity in the protein composition of molluscan and mammalian peroxisomes as revealed by the present study indicates that those proteins have been well conserved in evolution suggesting that functionally peroxisomes in molluscs could also be involved in the metabolism of lipids and in detoxification of xenobiotics. Thus, the antibodies tested could provide useful tools for detection of peroxisomal induction in molluscan biomonitoring programs for the assessment of aquatic environmental pollution.
    Type of Medium: Electronic Resource
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