FLUORESCENCE STUDIES OF COENZYME BINDING TO DEHYDROGENASES

Fluorescence studies of coenzyme-binding to beef heart lactic dehydrogenase.

Among the many methods which are available for studying the binding of substances to proteins (l), those applied most commonly for pyridine nucleotide-binding to dehydrogenases have been the spectrophotometric (2) and ultracentrifuge measurements (3). An additional method has been introduced through the observations of Boyer and Theorell (4) who found that reduced diphosphopyridine nucleotide i...

Fatty acyl-coenzyme A dehydrogenases.

Pande, S. V. & Parvin, R. (1976) J. Biol. Chem. 251,6683-6691 Pearson, D. J. & Tubbs, P. K. (1976) Biochem. J. 105,953-963 Ramsay, R. R. & Tubbs, P. K. (1974) Biochem. SOC. Traits. 2, 1285-1286 Ramsay, R. R. & Tubbs, P. K. (1975) FEBSLetf. 54,21-25 Ramsay, R. R. & Tubbs, P. K. (1976) Eur. J. Biochem. 69,299-303 Robles-Valdes, C . , McCarry, J. D. &Foster, D. W. (1976)J. Biol. Chern. 251, 6007-6...

Coenzyme linked dehydrogenases of acetic acid bacteria.

Protein fluorescence of nicotinamide nucleotide-dependent dehydrogenases.

1. The decrease in the protein fluorescence (F) of Neurospora crassa glutamate dehydrogenase is linearly related to the increase in the fraction of the coenzyme sites occupied by NADPH (alpha) at pH6.35. Under these conditions NADPH causes this enzyme to dissociate to monomers. 2. There is a non-linear relationship of F to alpha for NADH binding to give the alcohol dehydrogenase-NADH-isobutyram...

Intrinsic fluorescence studies on saccharide binding to Artocarpus integrifolia lectin.

The combining region of Artocarpus integrifolia lectin has been studied by using the ligand-induced changes in the fluorescence of the lectin. The saccharide binding properties of the lectin show that C-1, C-2, C-4, and C-6 hydroxyl groups of D-galactose are important loci for sugar binding. The alpha-anomer of galactose binds more strongly than its beta-counterpart. Inversion in the configurat...