Mechanism of activation of Na, K-ATPase in nerve fibres during rhythmic excitation.
The mechanism of activation of Na, K-ATPase in nerve fibres during rhythmic excitation was studied. 3H-ouabain binding to the nerve was found to be dependent on the frequency of rhythmic excitation. During rhythmic excitation 3H-ouabain binding was increased in all nerves tested. The maximum of 3H-ouabain binding in squid and crab nerves was observed at 10 impulses/s, and in frog nerve at 100 impulses/s. The level of bound glycoside decreased during high-frequency excitation. Rhythmic excitation did not change Na, K-ATPase affinity to ouabain, but it appeared to increase the concentration of ouabain sensitive sites in the nerve membrane. The enhancement of 3H-ouabain binding to nerve during rhythmic excitation is interpreted as arising from transformation of "inactive" forms of the enzyme to "active" ones.
Maximov
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GV
Kols
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D000818:Animals; D003386:Brachyura / Q000502:physiology; D049832:Decapodiformes / Q000502:physiology; D004558:Electric Stimulation; D004789:Enzyme Activation; D008297:Male; D009412:Nerve Fibers / Q000201:enzymology*; D010042:Ouabain / Q000494:pharmacology; D011188:Potassium / Q000378:metabolism; D011896:Rana temporaria / Q000502:physiology; D012964:Sodium / Q000378:metabolism; D000254:Sodium-Potassium-Exchanging ATPase / Q000037:antagonists & inhibitors / Q000378:metabolism*
D010042:Ouabain; D012964:Sodium; D000254:Sodium-Potassium-Exchanging ATPase; D011188:Potassium