Open AccessDihydropteridine Reductase
Author(s) -
Lind Kirsten E.
Publication year - 1973
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1973.tb02655.x
Subject(s) - dissociation constant , chemistry , quenching (fluorescence) , cofactor , fluorescence , enzyme , biochemistry , physics , receptor , quantum mechanics
Binding of NADH and quinoid dihydropteridine to dihydropteridine reductase from rat liver has been studied by the techniques of protein fluorescence quenching and ligand protection. The dissociation constans obtained for the binary complexes by the two methods were in agreement. For NADH, the constant was 0.07 μM and for quinoid dihydropteridine, 2–3 μM (30 °C, pH 6.8). The constants have been compared with the apparent Michaelis constants.