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 x 10(-3) M acetylcholine and Km of 1.6 x 10(-4) M, relative sensitivity to the specific inhibitors BW284C51 (I50 of 5 x 10(-8) M) and Iso-OMPA (I50 of 5 x 10(-4) M), and a half maximal thermal inactivation at 62.5 degrees 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.
journal_name
Neurochem Resjournal_title
Neurochemical researchauthors
Fernandez HLdoi
10.1007/BF00965031subject
Has Abstractpub_date
1981-09-01 00:00:00pages
1005-17issue
9eissn
0364-3190issn
1573-6903journal_volume
6pub_type
杂志文章abstract::Anesthetics such as propofol can provide neuroprotective effects against cerebral ischemia. However, the underlying mechanism of this beneficial effect is not clear. Therefore, we subjected male Sprague-Dawley rats to 2 h of middle cerebral artery occlusion and investigated how post-ischemic administration of propofol...
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