[Thiamine triphosphatase activity in mammalian mitochondria].
Mitochondrial preparations isolated from bovine kidney and brain as well as the liver and the brain of rat show thiamine triphosphatase (ThTPase) activity. The activity was determined from the particles by freezing-thawing suggesting that a soluble enzyme is involved. The liberation patterns of ThTPase and marker enzyme activities from mitochondria under osmotic shock or treatment with increasing Triton X-100 concentrations indicate the presence of ThTPase both in the matrix and intermembrane space. It was found, basing on gel filtration behavior, that the mitochondrial ThTPase has the same molecular mass as specific cytosolic ThTPase (EC 3.6.1.28). The enzymes, however, were clearly distinguishable in Km values, the mitochondrial one showing a higher apparent affinity for substrate. These results imply the existence of ThTPase multiple forms in mammalian cells.
Rusina
I M
IM
Institute of Biochemistry, National Academy of Sciences of Belarus, Grodno.
Makarchikov
A F
AF
D000818:Animals; D001921:Brain / Q000201:enzymology / Q000378:metabolism; D002417:Cattle; D003600:Cytosol / Q000201:enzymology; D005109:Extracellular Matrix / Q000201:enzymology; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D007668:Kidney / Q000201:enzymology / Q000378:metabolism; D008099:Liver / Q000201:enzymology / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology*; D051381:Rats; D013837:Thiamin-Triphosphatase / Q000378:metabolism*
D013837:Thiamin-Triphosphatase