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Content and binding characteristics of the mitochondrial ATPase inhibitor, IF-1, in the tissues of several slow and fast heart-rate homeothermic species and in two poikilotherms



Content and binding characteristics of the mitochondrial ATPase inhibitor, IF-1, in the tissues of several slow and fast heart-rate homeothermic species and in two poikilotherms



Journal of Bioenergetics and Biomembranes 27(1): 117-125



We determined the IF-1 contents of pig, rabbit, rat, mouse, guinea pig, pigeon, turtle, and frog heart mitochondria and the effects of varying ionic strength upon the IF-1-mediated inhibition of the ATPase activity of IF-1-depleted rabbit heart mitochondrial particles (RHMP) by IF-1-containing extracts from these same eight species. The IF-1 binding experiments were run at both species-endogenous IF-1 levels and at an IF-1 level normalized to that present in rabbit heart mitochondria. When species-endogenous levels of rabbit heart IF-1 or either species-endogenous or normalized levels of pig heart IF-1 were incubated with RHMP over a range of KCl concentrations, increasing the (KCl) to 150 mM had relatively little effect on IF-1-mediated ATPase inhibition. When either species-endogenous or normalized levels of guinea pig, pigeon, turtle, or frog heart IF-1 were incubated with RHMP under the same conditions, increasing (KCl) to 150 mM nearly completely blocked IF-1-mediated ATPase inhibition. While species-endogenous levels of rat and mouse heart IF-1 inhibited the ATPase activity of RHMP virtually not at all at any (KCl) examined, normalized levels of rat and mouse IF-1 inhibited the ATPase activity of RHMP to the same extents as species-endogenous levels of pig and rabbit heart IF-1, respectively, in the presence of increasing (KCl). These experiments suggest that, while pig and rabbit heart mitochondria contain a full complement of higher-affinity IF-1, pigeon, guinea pig, turtle, and frog heart mitochondria cell contain essentially a full complement of a lower-affinity form of IF-1. In contrast, rat and mouse heart mitochondria contain only low levels of IF-1 which exhibit binding characteristics similar to those of the pig and rabbit heart inhibitor. The guinea pig is the only mammal thus far examined that contains a lower-affinity form of IF-1. In the present study we also determined the IF-1 contents and IF-1-to-F-1-ATPase activity ratios of cardiac muscle, skeletal muscle, liver, and brain mitochondria of rabbit, pigeon, and rat, species representative of the three homeothermic regulatory classes.

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Accession: 008380648

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PMID: 7629043

DOI: 10.1007/bf02110339


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