Spermine effect on the binding of casein kinase I to the rat liver mitochondrial structures.

The results indicated here, together with those previously reported, show that spermine, ubiquitous polyamine, while promoting the transmembrane translocation of casein kinase II (CKII) across the outer membrane to more internal compartments of rat liver mitochondria, promotes the binding of casein kinase I (CKI) to the external surface of outer mitochondrial membrane but inhibits its spontaneously occurring binding to more internal structures.

Spermine-mediated casein kinase II-uptake by rat liver mitochondria.

Spermine, ubiquitous intracellular polyamine, is able to promote the transmembrane translocation of casein kinase CKII through the outer membrane of rat liver mitochondria and its binding to more internal mitochondrial structures. These findings suggest that spermine may play a critical role in regulating the subcellular distribution of casein kinase CKII.

Anaplerotic effect of propionyl carnitine in rat heart mitochondria.

Carnitine and propionyl carnitine both increase production of 14CO2 from [1-14C]pyruvate but only the latter, in a process inhibited by malonate, increases oxygen uptake and 14CO2 evolution from [2-14C]pyruvate. Carnitine increases the rate of formation of acetyl carnitine from pyruvate to a greater extent than propionyl carnitine. These effects of carnitine and propionyl carnitine are not detectable in mitochondria (e.