Poster Presenter

RNA-Hydrolyzing Activity Of Human Serum Albumin And Its Recombinant Analog
Tatyana Godovikova, Yulia Gerasimova, Tatyana Bobik and Natalya Ponomarenko
Russia

Human serum albumin (HSA) is a biological macromolecule that has a potential for a wide range of pharmaceutical applications. Due to its remarkably long half-life in a bloodstream, its wide in vivo distribution, HSA is an ideal carrier for therapeutic biological molecules that interact with cellular components. A remarkable functional property of albumin is its promiscuous catalytic activity toward a broad range of organic molecules.

In this study the comparative analysis of RNA-hydrolyzing activity of albumin from human serum and albumin expressed in methylotrophic yeast Pichia pastoris has been carried out. The rate of phosphodiester bonds cleavage in the presence of recombinant albumin has been found to be similar to that for the reaction mediated by the natural protein. Non-enzymatic glycation and N homocysteinylation of protein resulted in significant loss of its RNA-hydrolyzing activity.

Catalytic activity and substrate specificity of albumin in the reaction of RNA hydrolysis distinguish it from human ribonucleases. Although albumin displays a low reactivity toward RNA compared to human RNases, the large quantity of albumin in blood circulation and lymph may provide a substantial reservoir for sequestering and hydrolyzing extracellular nucleic acids.

The research is supported by integration grant #88 and RFBR grant #09-04-01483.