A 5′-phosphodiesterase activity from barley rootlets has been partially purified. Acetone precipitation up to 60% and DEAE-Sepharose chromatography are the two steps of the purification sequence. Thermal treatments as well as Sephadex G-100 chromatography were also assayed but results were not useful for the work purposes. Special consideration in phosphomonoesterase activity diminution in an economical way has been considered to select the purification procedure. Final results achieved are a degree of purification about 70 and a 5′-phosphodiesterase activity solution with 87 UA mg-1 protein. Tests of the final 5′-phosphodiesterase solution to be useful to degrade RNA to obtain mainly 5′-ribonucleotides from yeast RNA have been made. © 1989.
|Journal||Enzyme and Microbial Technology|
|Publication status||Published - 1 Jan 1989|
- barley rootlets