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. 1974 Sep;142(3):555–566. doi: 10.1042/bj1420555

A re-evaluation of energy-independent calcium-ion binding by rat liver mitochondria

Ken C Reed 1,*, Fyfe L Bygrave 1
PMCID: PMC1168319  PMID: 4219276

Abstract

The impermeability of the mitochondrial inner membrane to the chelator ethanedioxybis(ethylamine)tetra-acetic acid permits discrimination between Ca2+ which has been transported to the internal (matrix) phase and Ca2+ which binds to the external surfaces of the mitochondrion. With this technique, it is shown that `energy-independent high-affinity' binding is a measure of carrier-mediated active Ca2+ transport in respiration-inhibited mitochondria; the carrier also transports Ca2+ to the internal phase after treatment with carbonyl cyanide m-chlorophenylhydrazone, but in this case the active-transport component is inhibited. The Ca2+-binding sites associated with the external membrane surfaces are similar in concentration and affinity for both inhibited and uncoupled mitochondria; it was not possible to measure external Ca2+ binding which could be identified as carrier specific. The results are discussed in relation to the mechanism of mitochondrial Ca2+ transport, and to previous studies of energy-independent Ca2+ binding.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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