Collect. Czech. Chem. Commun. 1979, 44, 3327-3340

Nucleolytic enzymes of rape seedlings II. Unspecific acid phosphomonoester hydrolase

Ivan Rosenberg and Antonín Holý

Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Sciences, 166 10 Prague 6


Aqueous extracts of rape seedlings (Brassica napus L.) display phosphomonoesterase activity. The enzyme was purified gradually by chromatography on tert-butyl ester of Cellex P, affinity chromatography on sepharose 4B with linked p-aminophenyl(phenyl)thiophosphate or N6-(6-aminohexyl)adenosine 2'(3')-thiophosphate (final degree of purification 269x). The enzyme displayed activity toward various ribo- and 2'-deoxyribonucleotides, with preference for 3'-ribonucleotides, and to aryl or alkyl esters of phosphoric acid, ADP, ATP, inorganic pyrophosphate, as well as to nucleotide analogues containing acids of phosphorus with a small substituent on the phosphorus atom. The internucleotidic linkages of RNA and DNA are resistent. The enzyme is classified as an orthophosphate monoester hydrolase (EC