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Journal archive > 2009 > N 3 May-June

CHARACTERIZATION OF THIAMINE TRIPHOSPHATASE ASSOCIATED
WITH NEURAL CELLS PLASMA MEMBRANES

A. Sydorova, S. Stepanenko, Iu. M. Parkhomenko

Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
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The kinetic parameters of the ThTP hydrolysis by synaptic plasma membranes isolated from rat brain were investigated. It was shown that the ThTPase­ reaction pH optimum was 7.4, the apparent Кm was 52 µM and the apparent affinity constant for Мg2+ was 1.9 mM.
The comparative analysis of the indicated parameters was done for the ThTPase activity of membrane bound (the data of present work and literature data) and cytosolic (literature data) proteins. The analysis allows us to suppose that thiamine-binding protein described earlier is the sing­le ThTPase activity carrier in neural cells plasma membranes.
It was shown that the active site of the enzyme that catalyzes the ThTP hydrolysis in neural cells plasma membranes is associated with the inside membrane surface.

Key words: thiamine, thiamine triphosphate, thiamine triphosphatase, synaptic plasma membranes, thiamine-binding protein.

The original article in Russian is available for download in PDF format.

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