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. 1982 Jan 15;202(1):163–169. doi: 10.1042/bj2020163

Studies on the nature of the high-affinity trialkyltin binding site of rat liver mitochondria.

A P Dawson, B G Farrow, M J Selwyn
PMCID: PMC1158086  PMID: 7082305

Abstract

1. The proteolipid fraction isolated from rat liver mitochondria pretreated with [3H]triphenyltin chloride is enriched in triphenyltin compared with the original mitochondria. 2. Part of this [3H]triphenyltin is eluted with a protein of Mr 5000-6000 on Sephadex LH20 chromatography. 2. Mössbauer spectra of the proteolipid fraction treated with 119Sn-enriched triethyltin chloride show a doublet which corresponds closely with that assigned previously [Farrow & Dawson (1978) Eur. J. Biochem. 86. 85-95] to the absorption of triethyltin bound to the high-affinity binding site of the mitochondrial ATPase.

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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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