Collect. Czech. Chem. Commun. 1979, 44, 3327-3340
https://doi.org/10.1135/cccc19793327

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

This article is part of serial Nucleolytic enzymes of rape seedlings.

Abstract

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 3.1.3.2).