Abstract 1. The occurrence of an AMPase associated with cytomembranes has been demonstrated in the systemic heart of OctopusvulgarisLam. 2. At least two enzymes with different properties contribute to this activity: particularly one enzyme has the characteristics of a 5′-nucleotidase. 3. This enzyme is inhibited by AMPCP, Con-A, Ca2+ and EDTA, while it is strongly activated by Mg2+. 4. Its maximal activity is detectable over a range of pH from 6.6 to 8.5 and its affinity for AMP is very high . 5. GMP appears to be a competing substrate, while β-glycerophosphate is not.
Evidence For 5'-nucleotidase Activity In the Heart of Octopus-vulgaris Lam / M., Sciurba; Agnisola, Claudio; L., Foti; I. T., Genoino. - In: COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY. B, COMPARATIVE BIOCHEMISTRY. - ISSN 0305-0491. - STAMPA. - 80:(1985), pp. 67-72. [10.1016/0305-0491(85)90424-9]
Evidence For 5'-nucleotidase Activity In the Heart of Octopus-vulgaris Lam
AGNISOLA, CLAUDIO;
1985
Abstract
Abstract 1. The occurrence of an AMPase associated with cytomembranes has been demonstrated in the systemic heart of OctopusvulgarisLam. 2. At least two enzymes with different properties contribute to this activity: particularly one enzyme has the characteristics of a 5′-nucleotidase. 3. This enzyme is inhibited by AMPCP, Con-A, Ca2+ and EDTA, while it is strongly activated by Mg2+. 4. Its maximal activity is detectable over a range of pH from 6.6 to 8.5 and its affinity for AMP is very high . 5. GMP appears to be a competing substrate, while β-glycerophosphate is not.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
