ABSTRACT
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 polyribonucleotide phosphodiester bond cleavage in the presence of recombinant albumin has been found to be similar to that of the reaction mediated by the native protein. According to 31P NMR data, RNA hydrolysis follows the mechanism of intermolecular trans-esterification to yield 2',3'-cyclophosphodiester reaction products that are further slowly hydrolyzed to form nucleoside-3'- and nucleoside-2'-phosphates. Analysis of pH dependence suggests an acid-base mechanism of catalysis. The catalytic activity and substrate specificity of albumin in RNA hydrolysis distinguish it from human ribonucleases.
