Acylphosphatase is a widespread cytosolic enzyme that catalyzes the hydrolysis of carboxylphosphate bond compounds. Among natural acylphosphates hydrolyzed by the enzyme are 3-phosphoglyceroylphosphate, carbanoylphosphate, succinoylphosphate . In mammalian tissues acylphosphatase exists in two isoenzymatic forms: one is prevalent in skeletal muscle, the other in red blood cells (RBCs) . The physiological function of acylphosphatase is still debated.It has been postulated that, by hydrolyzlng 3-phosphoglyceroylphosphate' acylphosphatase may hasten glycolysis at the expence of ATP formation, when the rate of this pathway is limited by low concentrations of inorganic phosphate and ATP. In a recent research project we investigated acylphosphatase content and activity during the human erythrocyte lifespan

Acylphosphatase and calcium transport across erythrocyte membrane / NEDIANI C; G. LIGURI; TADDEI N; MARCHETTI E; RAMPONI G; NASSI P.. - STAMPA. - (1991), pp. 207-215.

Acylphosphatase and calcium transport across erythrocyte membrane.

NEDIANI, CHIARA
;
LIGURI, GIANFRANCO;TADDEI, NICCOLO';RAMPONI, GIAMPIETRO;NASSI, PAOLO ANTONIO
1991

Abstract

Acylphosphatase is a widespread cytosolic enzyme that catalyzes the hydrolysis of carboxylphosphate bond compounds. Among natural acylphosphates hydrolyzed by the enzyme are 3-phosphoglyceroylphosphate, carbanoylphosphate, succinoylphosphate . In mammalian tissues acylphosphatase exists in two isoenzymatic forms: one is prevalent in skeletal muscle, the other in red blood cells (RBCs) . The physiological function of acylphosphatase is still debated.It has been postulated that, by hydrolyzlng 3-phosphoglyceroylphosphate' acylphosphatase may hasten glycolysis at the expence of ATP formation, when the rate of this pathway is limited by low concentrations of inorganic phosphate and ATP. In a recent research project we investigated acylphosphatase content and activity during the human erythrocyte lifespan
1991
Red Blood Cell Aging
207
215
NEDIANI C; G. LIGURI; TADDEI N; MARCHETTI E; RAMPONI G; NASSI P.
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Utilizza questo identificatore per citare o creare un link a questa risorsa: https://hdl.handle.net/2158/309880
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