Interaction of AMP with cytosolic apo-aspartate aminotransferase.
作者信息
Di Donato A, Fiore R, Garzillo A M, Marino G
出版信息
FEBS Lett. 1983 Mar 7;153(1):98-102. doi: 10.1016/0014-5793(83)80126-4.
PMID:6825864
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 10(-6) M-1 and 31.4 x 10(-6) M-1, respectively. These findings substantiate a previous hypothesis of control of the reconstitution of cytosolic apo-aspartate aminotransferases exerted by AMP.
摘要
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