Reaction of mersalyl with mitochondrial proteins under native and denaturing conditions as exemplified by the identification and isolation of the phosphate carrier.
Pig heart mitochondria were incubated with [203Hg]mersalyl and the radioactive pattern was analyzed by fluorography after dodecyl sulfate gel electrophoresis. No differences in the radioactivity distribution were found after labeling with various mersalyl concentrations, at different pH and after labeling in the native or dodecyl sulfate-dissociated state of mitochondria. A redistribution of [203Hg]mersalyl between various proteins in the presence of dodecyl sulfate could directly be demonstrated by mixing labeled membranes with unlabeled matrix proteins, as well as by comparison of the radioactivity patterns of whole mitochondria labeled with irreversibly reacting N-([2-3H]ethyl)maleimide and reversibly binding [203Hg]mersalyl. From these data it is concluded that under native conditions mersalyl is principally bound to the phosphate carrier protein, whereas during dissociation in dodecyl sulfate the organomercurial is redistributed and mainly attached to the ADP/ATP-carrier protein.
D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification*; D008634:Mersalyl / Q000378:metabolism*; D008929:Mitochondria, Heart / Q000378:metabolism*; D009941:Organomercury Compounds / Q000378:metabolism*; D028044:Phosphate-Binding Proteins; D010710:Phosphates / Q000378:metabolism*; D011489:Protein Denaturation; D013552:Swine
D002352:Carrier Proteins; D009941:Organomercury Compounds; D028044:Phosphate-Binding Proteins; D010710:Phosphates; D008634:Mersalyl