Section of Biochemistry, Molecular and Cell Biology Cornell University, Ithaca, New York 14853 USA
Abstract:
Phosphate transporter of bovine heart mitochondria was purified by solubilization of submitochondrial particles with octylglucoside and fractionation of the extract with ammonium sulfate. After reconstitution into liposomes the purified protein catalyzed phosphate transport which was sensitive to mersalyl and other SH reagents. Transport measured either as or exchange was proportional to protein concentration and time. The but not the exchange was stimulated several fold by valinomycin plus nigericin in the presence of K+. The reconstituted system provides a suitable assay during purification of the mitochondrial phosphate transporter.