Peter H W, Pinheiro M R, Silva Lima M
Can J Biochem. 1981 Jan;59(1):60-6. doi: 10.1139/o81-009.
Mitochondria from Vigna sinensis (L.) Savi cv. Pitiuba contain the polyamines spermine, spermidine, and putrescine. The membrane-bound F1-ATPase from mitochondria of Vigna sinensis is activated by these polyamines at physiological concentrations. The effect of polyamines on the membrane-bound of F1-ATPase is dependent on the concentrations of Na+, K+, MgATP, and Mg2+. Excess Na+ or K+ prevents the activation of the membrane-bound F1-ATPase by spermine and spermidine, but not by putrescine. The most pronounced effects were observed at low MgATP concentrations in the absence of Na+ and K+. At [MgATP] = 0.08 mM, spermine activation of the membrane-bound F1-ATPase was 130%. The membrane-bound F1-ATPase is slightly activated by Mg2+ at lower concentrations and strongly inhibited by Mg2+ at higher concentrations. Activation as well as inhibition is dependent on the substrate MgATP concentration. Although there is competition between Mg2+ and MgATP, the binding sites for these two ligands are different (pseudocompetitive inhibition). The inhibition of the membrane-bound F1-ATPase can be reversed by polyamines. There is evidence that the binding sites for Mg2+ and polyamines are identical. The F1-ATPase detached from the membrane is neither activated by polyamines nor inhibited by Mg2+. Therefore, the binding sites for Mg2+ and polyamines seem to be localized on the membrane.
来自豇豆（Vigna sinensis (L.) Savi cv. Pitiuba）的线粒体含有多胺精胺、亚精胺和腐胺。豇豆线粒体膜结合的F1 - ATP酶在生理浓度下会被这些多胺激活。多胺对膜结合F1 - ATP酶的作用取决于Na +、K +、MgATP和Mg2 +的浓度。过量的Na +或K +会阻止精胺和亚精胺对膜结合F1 - ATP酶的激活，但腐胺不会。在没有Na +和K +的情况下，在低MgATP浓度时观察到最显著的影响。当[MgATP] = 0.08 mM时，精胺对膜结合F1 - ATP酶的激活率为130%。膜结合F1 - ATP酶在较低浓度的Mg2 +下会被轻微激活，而在较高浓度下会被强烈抑制。激活和抑制都取决于底物MgATP的浓度。虽然Mg2 +和MgATP之间存在竞争，但这两种配体的结合位点不同（伪竞争性抑制）。膜结合F1 - ATP酶的抑制作用可以被多胺逆转。有证据表明Mg2 +和多胺的结合位点是相同的。从膜上分离的F1 - ATP酶既不会被多胺激活，也不会被Mg2 +抑制。因此，Mg2 +和多胺的结合位点似乎位于膜上。
