Tomoaki Yoshioka

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The technique for covalently labeling proteins with 125I-labelled Bolton-Hunter reagent was used to determine the quantities of proteins released from the axoplasmic side of the squid axon membrane. The reagent could be introduced into the interior of the axon by the technique of intracellular perfusion, the radioiodination reaction being carried out in(More)
Single crystals of a macrocyclic hydro-carbon, [6]cyclo-2,7-naphthyl-ene ([6]CNAP, C(60)H(36)) were prepared from anthracene melt with a prolonged time for the recrystallization. The crystal of improved quality led to the correction of the space-group assignment to Cmca from [Formula: see text] in the original determination [Nakanishi et al. (2011 ▶) Angew.(More)
Proteins in the squid giant axon were labeled with 32P by in vitro incubation of isolated axoplasm with radioactive [gamma-32P]adenosine triphosphate (ATP) and separated by polyacrylamide sodium dodecyl sulfate gel electrophoresis. The two major phosphorylated regions on the gel had molecular weights of 400,000 and 200,000. These two peaks appear to be(More)
In vitro and in situ (after intracellular infusion) incubation of axoplasm from the squid giant axon with [gamma-32P]ATP produces a phosphorylation of primarily two proteins (of mol.wt. 200,000 and greater than 400,000). The phosphorylation of these proteins is stimulated by Mg2+, inhibited by Ca2+, and unaffected by 10(-7) to 10(-5) M cyclic nucleotides.(More)
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