Studies on the nature of the high-affinity trialkyltin binding site of rat liver mitochondria.
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.
D000818:Animals; D001665:Binding Sites; D002850:Chromatography, Gel; D066298:In Vitro Techniques; D008081:Liposomes / Q000378:metabolism; D008930:Mitochondria, Liver / Q000378:metabolism*; D009947:Organotin Compounds / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism; D011510:Proteolipids / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D013053:Spectrophotometry
D008081:Liposomes; D009947:Organotin Compounds; D010743:Phospholipids; D011510:Proteolipids; C012594:triphenyltin chloride