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Characterization of a novel nucleolytic activity of acylphosphatases
Author(s) -
Chiarugi Paola,
Raugei Giovanni,
Fiaschi Tania,
Taddei Letizia,
Camici Guido,
Ramponi Giampietro
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201552
Subject(s) - ribonuclease , biochemistry , deoxyribonuclease , nucleic acid , enzyme , dna , gene isoform , chemistry , biology , rna , gene
A novel enzymatic activity on nucleic acids was discovered in both muscle type (MT) and erythrocyte or common type (CT) isoforms of acylphosphatase, an enzyme that was previously known as a hydrolase (E.C.3.6.1.7). Both deoxyribonucleic and ribonucleic hydrolitic activity were assayed on a variety of substrates. Our results demonstrate that acylphosphatase possesses both Mg++ dependent deoxyribonuclease and ribonuclease acivities, at pH ranging from 5.0 to 6.8. Furthermore, we present evidences, for both isoenzymatic forms, of the coexistence of exonucleolytic and endonucleolytic activities on DNA.