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Ichiji Tasaki
Researcher at National Institutes of Health
Publications - 122
Citations - 5299
Ichiji Tasaki is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Squid giant axon & Squid. The author has an hindex of 36, co-authored 122 publications receiving 5156 citations. Previous affiliations of Ichiji Tasaki include Marine Biological Laboratory & Keio University.
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An approach to the study of intracellular proteins related to the excitability of the squid giant axon.
TL;DR: 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, finding that proteins of approx.
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Mechanical and thermal changes in the Torpedo electric organ associated with its postsynaptic potentials.
TL;DR: Rapid mechanical and thermal changes in slices of the Torpedo electric organ evoked by electric stimulation were investigated and the organ was found to swell simultaneously with the postsynaptic potential, followed by prolonged shrinkage of the organ.
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Intracellular Perfusion of Chilean Giant Squid Axons
Ichiji Tasaki,Mario Luxoro +1 more
TL;DR: Axons of the Chilean giant squid were subjected to continuous intracellular perfusion with either potassium- or sodium-rich salt solutions, and action potentials were observed which exceeded the value calculated from the Nernst equation applied to sodium-ion activity.
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Divalent cation dependent phosphorylation of proteins in squid giant axon.
TL;DR: 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, and phosphorylated peaks in situ is decreased by electrical stimulation of the axon.
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Protein release from the internal surface of the squid giant axon membrane during excitation and potassium depolarization
TL;DR: Observations indicate that there exists, in close association with the axonal membrane, aparticular group of proteins, the solubility of which is readily affected by changes in the state of the membrane.