Interaction of cytosolic apo-aspartate aminotransferase with AMP has been studied under equilibrium conditions; e.g., equilibrium dialysis and spectrophotometric titration. Results show that a 1 : 1 stoichiometric complex AMP-apo-aspartate aminotransferase monomer is formed. The calculated dissociation constants with the two different experimental techniques are 40.4 x 10m6 M-1 and 31.4 x 10m6 M-1, respectively. These findings substantiate a previous hypothesis of control of the reconstitution of cytosolic apo-aspartate aminotransferases exerted by AMP.
Interaction of AMP with Cytosolic Apo-Aspartate Aminotransferase / DI DONATO, Alberto; Fiore, R.; Garzillo, A. M.; Marino, Gennaro. - In: FEBS LETTERS. - ISSN 0014-5793. - STAMPA. - 153:(1983), pp. 98-102.
Interaction of AMP with Cytosolic Apo-Aspartate Aminotransferase
DI DONATO, ALBERTO;MARINO, GENNARO
1983
Abstract
Interaction of cytosolic apo-aspartate aminotransferase with AMP has been studied under equilibrium conditions; e.g., equilibrium dialysis and spectrophotometric titration. Results show that a 1 : 1 stoichiometric complex AMP-apo-aspartate aminotransferase monomer is formed. The calculated dissociation constants with the two different experimental techniques are 40.4 x 10m6 M-1 and 31.4 x 10m6 M-1, respectively. These findings substantiate a previous hypothesis of control of the reconstitution of cytosolic apo-aspartate aminotransferases exerted by AMP.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
