Comparison of the properties of purified mitochondrial and cytosolic rat kidney transamidinase.

ABSTRACT

1. Mitochondrial rat kidney transamidinase was solubilized by two extractions with the surfactant Zwittergent 3-14. 2. Mitochondrial and cytosolic forms of rat kidney transamidinase were purified by chromatography on DEAE-Trisacryl M, phenyl-Sepharose Cl-4B and hydroxylapatite columns. 3. The specific activity of purified mitochondrial enzyme was significantly higher than purified cytosolic enzyme. 4. The subunit molecular mass, the electrophoretic mobility under nondenaturing conditions, and the activation energy were similar for purified mitochondrial and cytosolic transamidinase.