Purification and characterization of acid phospho di esterases ec 3.1.4 of cultured tobacco nicotiana tabacum cultivar bright yellow cells

Matsuzaki, H.; Hashimoto, Y.

Agricultural and Biological Chemistry 45(6): 1317-1326

1981


ISSN/ISBN: 0002-1369
Accession: 006226125

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Abstract
Two acid phosphodiesterases (phosphoric diester hydrolase, EC 3.1.4.-) were purified to apparent homogeneity from cultured cells of N. tabacum cv. Bright Yellow. These enzymes appeared to differ in some physicochemical properties but exhibited similar broad substrate specificities towards cyclic and p-nitrophenyl nucleotides and bis-p-nitrophenyl phosphate. Of these compounds, the most active substrates were bis-p-nitrophenylphosphate and 2',3'-cyclic nucleotides. Both p-nitrophenyl 3'- and 5'-thymidylates were hydrolyzed at comparable rates; the hydrolysis of 3',5'-cAMP occurred preferentially at the 5'-phosphodiester bond. A unique catalytic property of these acid phosphodiesterases was the ability to liberate Pi from ATP, ADP and p-nitrophenyl phosphate. RNA, its breakdown products and Pi were effective as inhibitors.