نتایج جستجو برای: torpedo
تعداد نتایج: 1676 فیلتر نتایج به سال:
approved:_ __ Lavern J. Weber Neuromuscular pharmacology has been extensively studied in mammals but there have been few investigations examining the neuromuscular systems of fish. In situ experiments have shown that the basic cholinergic characteristics of fish neuromuscular junctions are different from those of mammals. In order to further understand the nature of these differences, the riico...
Studies on the electric organs of Narcine brasiliensis and particularly of the responses of the electroplaques of the accessory organ confirm and amplify data obtained on the electroplaques of Torpedo nobiliana. Only the innervated surface is electrogenically reactive and the uninnervated surface has a low resistance, as in Torpedo electroplaques. However, in the accessory organ of Narcine the ...
Torpedo californica electric organ cDNA libraries were constructed in lambda gt10 and lambda gt11. Four acetylcholine receptor (AcChoR) subunit cDNA clones were isolated and shown to contain the entire coding region for each of the subunits. When in vitro synthesized AcChoR mRNA was microinjected into Xenopus laevis oocytes, functional cell surface AcChoRs were expressed. A very simple and fast...
A peptide of acetylcholinesterase (AcChoEase; acetylcholine acetylhydrolase, EC 3.1.1.7) from the venom of the cobra Naja naja oxiana labeled by the affinity reagent N,N-dimethyl-2-phenylaziridinium (DPA) has been identified. The sequence is Gly-Ala-Glu-Met-Trp-Asn-Pro-Asn. In AcChoEase from Torpedo californica, a homologous peptide was labeled and isolated. Its sequence is Ser-Gly-Ser-Glu-Met-...
DNA sequences coding for the muscle-specific subunit of creatine kinase have been isolated from cDNA libraries constructed from Torpedo marmorata electric organ. Clones were screened by differential in situ hybridization and hybrid-selected translation. The in vitro translation product of the selected mRNA was immunoprecipitated by anti-chicken creatine kinase antibodies and comigrated with Tor...
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