1) Evidence obtained from washout experiments of
45Ca ions in frog sartorius muscles has led to the conclusion that IAA promotes Ca
++ ion release from the muscle fibre surface. The detailed mechanism to produce the enhancement has been investigated from the viewpoint of a direct effect of IAA on membrane lipoprotein, especially on its SH groups.2) As the concentration of externally applied IAA was increased from a threshold concentration of about 0.1 mM, continuous increase in
45Ca efflux began to appear. Near 2 mM, the increase in
45Ca efflux was complicated by an addition of the reduction in it.3) The increase in
45Ca dissociation was presumed as a result of the effect of IAA on membrane SH groups, while the reduction in the same ion movement was supposed as failed glycolysis. Accordingly,
45Ca efflux increase by IAA was not a response to the drug but a sequence of the destruction of normal lipoprotein conformation. The experiments of
22Na efflux also proved that the increase in
22Na efflux due to IAA was a consequence of disorganization of chemical membrane architecture.4)
45Ca efflux increase by IAA was not short-lived but continuous. IAA prevented the appearance of immobilizing effect of trypsin on membrane
45Ca ions. DNFB demonstrated a marked transient increase in
45Ca dissociation. As far as the kinetic behaviors of membrane
45Ca ions are concerned, the sites of Ca
++ ions relating to IAA are clearly different from the sites of Ca
++ ions connecting to trypsinization or DNFB action.5)
45Ca ions mobilized by IAA are not Ca
++ ions extremely susceptible to the external Ca
++ ions, which directly govern the concentration of Ca
++ ions in the superficial layer of the membrane. When Sr
++ ions were used instead of Ca
++ ions in Ringer,
45Ca efflux was not stimulated by IAA, suggesting that the membrane structure maintaining properly by Ca
++ ions may be a premise for an enhanced Ca
++ efflux increase by IAA . The immobilizing effect of no external K
+ on
45Ca efflux was hardly seen in the presence of IAA.6) The structural change of methylative amino acids, playing important role in performing biosynthesis or maintenance of membrane phospholipid, especially lecithin, produced by IAA, probably results indirectly in labilization of membrane Ca
++ ions through rearrangement of the binding pattern altered secondary to conformational change in membrane lipoprotein.
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