Crystal-structure determination of reduced nicotinamide adenine dinucleotide complex with horse liver alcohol dehydrogenase maintained in its apo conformation by zinc-bound imidazole

Biochemistry ◽  
1983 ◽  
Vol 22 (25) ◽  
pp. 5761-5772 ◽  
Author(s):  
Eila Cedergren-Zeppezauer
Keyword(s):  
Crystal Structure ◽  
Alcohol Dehydrogenase ◽  
Structure Determination ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver ◽  
Reduced Nicotinamide Adenine Dinucleotide

Residual Fluorescence as an Index of Purity of Reduced Nicotinamide Adenine Dinucleotide

1973 ◽  
Vol 19 (11) ◽  
pp. 1280-1284 ◽  
Author(s):  
Barbara F Howell ◽  
Sam Margolis ◽  
Robert Schaffer
Keyword(s):  
Alcohol Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine ◽  
Rate Of Reaction ◽  
Optical Rotations ◽  
Reduced Nicotinamide Adenine Dinucleotide

Abstract Determination of fluorescence remaining after reduced nicotinamide adenine dinucleotide (NADH) has reacted with excess acetaldehyde in the presence of alcohol dehydrogenase (EC 1.1.1.1) is useful as a criterion of NADH purity when used in conjunction with other methods for determining purity such as the rate of reaction, the ratio of ultraviolet absorbances at 260 nm and 340 nm, the color, and the chromatographic homogeneity of the preparation. Measurement of residual fluorescence monitors the enzymatically inactive material which absorbs at 340 nm. The specific optical rotations of NADH at several wavelengths are also reported.

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