Seibutsu Butsuri
Online ISSN : 1347-4219
Print ISSN : 0582-4052
ISSN-L : 0582-4052
Volume 16, Issue 3
Displaying 1-3 of 3 articles from this issue
  • Kohtaro KAMINO, Akira INOUYE
    1976 Volume 16 Issue 3 Pages 113-125
    Published: May 25, 1976
    Released on J-STAGE: January 07, 2010
    JOURNAL FREE ACCESS
    In comparison with other excitable membranes, interactions with some ions of synaptosomal membranes in vitro were dealt with in the present review. Effects of external high K+ on synaptosomal Ca2+-binding and on Ca2+-influx of synaptosomes were reviewed. External high K+ induced the swelling of synaptosomes. Such phenomena were discussed in connection with the liberation of membrane-bound Ca2+ From the changes in extrinsic fluorescence, K+-induced depolarization of synaptosomal membrane was described. Based on these results, some changes in membrane structure and/or its permeability properties accompanied with depolarization were discussed. In addition, using spin-labels, changes in fluidity of synaptosomal membranes induced some ions were also described.
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  • Yasunobu OKADA, Akira INOUYE
    1976 Volume 16 Issue 3 Pages 126-135
    Published: May 25, 1976
    Released on J-STAGE: May 25, 2009
    JOURNAL FREE ACCESS
    The ionic permeabilities and conductive properties across intestinal epithelia were reviewed from the electrophysiological point of view. Based on our own data on the electrical parameters required for application of the equivalent circuit analysis, the contribution of an extracellular shunt conductance and that of an electrogenic sodium pump to the electrical properties of small intestine were estimated. In order to throw light upon the origin of a solute evoked potential changes, the changes in electrical parameters induced by an active solute transport were discussed.
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  • Hiroshi NAKATANI, Kazumitsu HANAI
    1976 Volume 16 Issue 3 Pages 136-143
    Published: May 25, 1976
    Released on J-STAGE: May 25, 2009
    JOURNAL FREE ACCESS
    Conformational change occurring in the enzyme and/or enzyme-ligand complexes has been suggested, and evidences for it have been obtained by X-ray crystallography for some enzymes.
    In the kinetic studies of enzyme-ligand interactions by the temperature-jump and stopped-flow methods, unimolecular isomerization processes of enzymes and/or enzyme-ligand complexes are frequently observed, which are attributable to a conformational change.
    Unimolecular isomerization processes may be classified as follows, A) Conformational change of the enzyme only E_??_E* B) Conformational change of the enzyme-ligand complexes E·S_??_E·S* E·S_??_E*·S E·S_??_E*·S* where the mark * shows the "deformated state" of the enzyme or the ligand (E= enzyme, and S=ligand).
    Examples for each case are reviewed for several enzymes including serine proteinases, lysozyme, RNAse, and aminoacylt-RNA synthetase.
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