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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    European archives of oto-rhino-laryngology and head & neck 238 (1983), S. 123-125 
    ISSN: 1434-4726
    Keywords: Otosclerosis ; Stapes footplate ; Cathepsin B
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Cathepsin-B activity was determined fluorimetrically in the otosclerotic stapes footplate, the stapes superstructure, normal temporal cortical bone, and os frontale osteoma. Measurements with a synthetic substrate made determinations in individual samples possible. The cathepsin-B activity in the otosclerotic stapes footplate was one order of magnitude higher than that of the superstructure, which was not affected by the disease. The cortical bone and the superstructure displayed similar activities, as did os frontale osteoma and otosclerosis. The high lysosomal proteinase activity appears to be closely connected to the otosclerotic bone resorption process.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    European archives of oto-rhino-laryngology and head & neck 243 (1986), S. 229-232 
    ISSN: 1434-4726
    Keywords: Myosin kinase ; Otosclerosis ; Perilymph ; Organ of Corti
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The guinea pig organ of Corti contains myosin light-chain kinase (MLCK) activity. The upper and lowermost parts of the cochlea do not show significantly different activities of the enzyme, which is Ca2+ and calmodulin-dependent. Short-term noise exposure does not cause a significant change. 0.3–5 Kilodalton substances of the otosclerotic perilymph, separated by SG-25 column chromatography, inhibit the MLCK activity in in vitro organ of Corti preparations. This inhibitory action of the perilymph substances can also be observed with the purified MLCK of turkey gizzard. The activity of the enzyme can be specifically inhibited by cyclic AMP-dependent protein kinase.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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