Abstract
Rabbit muscle aldolase binds NADPH with a 1:1 stoichiometry and with a dissociation constant 18 microM. Three sites of the dinucleotide are involved in the binding: the adenosyl diphosphate moiety, the nicotinamide-ribose, and the nicotinamide ring. These data show the existence of a specific dinucleotide binding site in the aldolase molecule.
Publication types
-
Comparative Study
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
Binding Sites
-
Chemical Phenomena
-
Chemistry
-
Fructose-Bisphosphate Aldolase / antagonists & inhibitors
-
Fructose-Bisphosphate Aldolase / metabolism*
-
In Vitro Techniques
-
Muscles / metabolism*
-
NADP / metabolism*
-
Rabbits
Substances
-
NADP
-
Fructose-Bisphosphate Aldolase