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- W1987248001 abstract "It is now well established that adenosine 5′-monophosphate (AMP) is a specific, allosteric, noncompetitive inhibitor of fructose 1,6-diphosphatase (FDPase) with cooperative interactions (1). However, our initial studies on the binding of 14C-AMP to rabbit liver FDPase using equilibrium dialysis, gel filtration, and density gradient ultracentrifugation failed to show any detectable binding in the absence of substrate. Further experiments proved that fructose 1,6-diphosphate (FDP) was an essential cooperative factor for AMP binding with the enzyme. This communication presents three lines of evidence in support of this conclusion." @default.
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- W1987248001 date "1968-03-01" @default.
- W1987248001 modified "2023-10-11" @default.
- W1987248001 title "Requirement of substrate for adenosine 5′-monophosphate binding to liver fructose 1,6-diphosphatase" @default.
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- W1987248001 doi "https://doi.org/10.1016/0006-291x(68)90569-x" @default.
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