Stepwise Synthesis of Oligonucleotides . XXXV. The Native and Immobilized Thermus thermophilus Polynucleotide Phosphorylase in the Oligoribonucleotide Synthesis
E. A. Sedel'nikova, O. A. Smolyaninova, S. M. Zhenodarova
Institute of Biological Physics, Academy of Sciences of the USSR, Pushchino , Moscow Region
Abstract: A polynucleotide phosphorylase was isolated from the Thermus thermophilus protein fractions, obtained at different steps of purification of elongation factors, and immobilized on agarose activated with cyanogen bromide and macroporous glass modified with (3,3-diethoxypropyl)triethoxysilane. The preparations of the native and immobilized enzyme catalized rather efficiently the addition of adcnylyl and guanylyl residues to oligonucleotide primers, in contrast to the E. coli and M. luteus polynucleotide phosphorylases. Tri-, tetra- and pentanucleotides with 3'-terminal guanosine and adenosine were obtained including structural analogues of the anticodon fragment 34—37 of yeast tRNAphe.
Russian Journal of Bioorganic Chemistry 1990, 16 (5):617-624