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  • 1980-1984  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 35 (1980), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The effects of certain protease inhibitors on end-plate acetyl-cholinesterase (AChE) activity, as well as on wet weight and total protein, were studied in vivo in intact and denervated anterior gracilis muscles from the rat. A combination of leupeptin, pepstatin, and aprotinin, administered intraarterially, partly prevented the early (24 h) denervation-induced decrease in muscle weight and protein content. In turn, leupeptin and aprotinin, either alone or in combination, markedly reduced the decay of AChE activity in the denervated muscles, whereas pepstatin alone was ineffective. Such effects were additive in that the inhibitors in combination were more effective than when they were used separately. Additional experiments indicated that none of the inhibitors, at the concentrations used, affected AChE activity directly, nor did they have a significant effect during processing of the muscle samples. These findings indicate that the initial decay of AChE activity with denervation was effectively reduced by the inhibitors, probably through inactivation of proteolytic enzymes which, otherwise, would be increased in denervated muscle.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-6903
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The characterization of individual acetylcholinesterase (AChE) molecular form subcellular pools in adult mammalian skeletal muscle is a critical point when considering such questions as the origin, assembly, and neurotrophic regulation of these molecules. By correlating the results of differential extraction, in vitro collagenase digestion, and in situ pharmacologic probes of AChE molecular forms in endplate regions of adult rat anterior gracilis muscle, we have shown that: 1) 4.0S (G1) and 6.0S (G2) AChE are predominantly membrane-bound and intracellular; if an extracellular and/or soluble fraction of these forms exists, it cannot be adequately resolved by our methods; 2) 9–11S (globular) AChE activity is distributed between internal and external pools, as well as membrane-associated and soluble fractions; 3) 16.0S (A12) AChE is not an integral membrane protein and exists both intracellularly (25–30%) and extracellularly (70–75%).
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Neurochemical research 6 (1981), S. 1005-1017 
    ISSN: 1573-6903
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Rat obturator nerve 16S acetylcholinesterase (16S AChE) was separated by sucrose gradient velocity sedimentation and compared to the 16S form of AChE similarly derived from endplate regions of anterior gracilis muscles. The 16S AChE from both tissues could only be extracted in high ionic strength buffer; as it aggregated under low ionic strength conditions. Treatment of nerve and muscle 16S AChE with purified collagenase, in the presence of calcium, caused an identical “shift” in the enzyme's sedimentation coefficient to 17.5S. Other properties which were also equivalent for 16S AChE from both tissue sources included: an excess substrate inhibition above 2×10−3 M acetylcholine andK m of 1.6×10−4 M, relative sensitivity to the specific inhibitors BW284C51 (I50 of 5×10−8 M) and Iso-OMPA (I50 of 5×10−4 M), and a half maximal thermal inactivation at 62.5°C. These and additional results indicate that the 16S forms of AChE in both tissues are analogous molecules, which have a highly asymmetric conformation probably containing a collagen-like domain. The present findings are also consistent with the view that motor neurons provide at least a fraction of the 16S AChE present at the neuromuscular junction.
    Type of Medium: Electronic Resource
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