Isolation and Physicochemical Properties of Tankyrase of Human Embryonic Kidney Cells of Line 293

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N. N. Sidorova¹, A. O. Fadeev², and A. N. Kuimov^1*

¹Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119992 Moscow, Russia; fax: (495) 939-3181; E-mail: kuimov@genebee.msu.su

²Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, 119992 Moscow, Russia

^* To whom correspondence should be addressed.

Received September 24, 2007; Revision received October 9, 2007

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We have isolated and purified endogenous cytosolic tankyrase from human embryonic kidney cells of line 293. Our data confirm a model of De Rycker and Price who consider that tankyrase is a master scaffolding protein capable of regulating assembly of large protein complexes. We have also studied kinetic characteristics of tankyrase in the complex, pH dependence of the enzyme activity, and its physicochemical properties.

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KEY WORDS: tankyrase, poly(ADP-ribose), PARP, ADP-ribosylation, kidney

DOI: 10.1134/S0006297908030085

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