Abstract: 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 activities, 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.
Characterization of a novel nucleolytic activity of acylphosphatases / P. Chiarugi; G. Raugei; T.Fiaschi; L. Taddei; G. Camici; G. Ramponi. - In: BIOCHEMISTRY AND MOLECULAR BIOLOGY INTERNATIONAL. - ISSN 1039-9712. - STAMPA. - 40:(1996), pp. 73-81.
Characterization of a novel nucleolytic activity of acylphosphatases
CHIARUGI, PAOLA;RAUGEI, GIOVANNI;FIASCHI, TANIA;TADDEI, MARIA LETIZIA;CAMICI, GUIDO;RAMPONI, GIAMPIETRO
1996
Abstract
Abstract: 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 activities, 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.I documenti in FLORE sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.