A. A. Kiladze

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The study of the melting characteristics of lactate dehydrogenase M4 and Zn/lactate dehydrogenase at pH 6.5-8.5 by microcalorimetric methods shows that in dilute solutions of the enzyme (0.05% lactate dehydrogenase solution) one Zn ion causes destabilisation of enzyme structure, attended by a decrease of melting temperature throughout the entire pH interval(More)
The effect of X-irradiation (1000 r) on the rat liver nuclear DNA Zn content has been studied. The results show a significant decrease of Zn content 1 hour after irradiation and some its normalization after 24 hours. The obtained data on Zn content decrease may be considered as one of the responses of nuclear DNA to irradiation.
ATPase melting has been studied by circular dichroism and differential scanning microcalorimetry. Decomposition of the α-helix of H+-ATPase (in which about 80% of the peptide groups of the enzyme are involved) following thermal treatment is shown to proceed gradually, beginning with room temperature. Effect of nucleotides upon melting is detected in the(More)
A zinc-binding nonmetallothionein protein has been isolated from cytosol of normal and regenerating liver. It is a dimer with molecular weight of ca. 20 kDa and contains one zinc ion. Zinc-dependent monomer in equilibrium dimer transition was observed. The role of the protein in regulation of intracellular content of zinc ions has been discussed.
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