Circular dichroism of complexes of NADH with self-associating bovine liver glutamate dehydrogenase

Biopolymers ◽  
1979 ◽  
Vol 18 (9) ◽  
pp. 2289-2301 ◽  
Author(s):  
Leila Zeiri ◽  
Emil Reisler
Keyword(s):  
Circular Dichroism ◽  
Glutamate Dehydrogenase ◽  
Bovine Liver ◽  
Circular Dichroïsm

scholarly journals The allosteric mechanism of bovine liver glutamate dehydrogenase. Evidence from circular-dichroism studies for a conformational change in the ternary complex enzyme-(oxidized nicotinamide-adenine dinucleotide)-glutarate

1977 ◽  
Vol 163 (2) ◽  
pp. 297-302 ◽  
Author(s):  
S S Chen ◽  
P C Engel ◽  
P M Bayley
Keyword(s):  
Circular Dichroism ◽  
Glutamate Dehydrogenase ◽  
Conformational Change ◽  
Circular Dichroism Spectrum ◽  
Direct Evidence ◽  
Bovine Liver ◽  
Substrate Analogues ◽  
Allosteric Mechanism ◽  
Nad 4 ◽  
Circular Dichroïsm

1. Computer averaging of multiple scans was used to refine the circular dichroism spectrum of bovine liver glutamate dehydrogenase, revealing well-defined structure in the aromatic region. 2. The circular dichroism of NAD+ bound to glutamate dehydrogenase is strongly negative at 260nm, probably owing to immobilization of the adenosine moiety. Loss of the characteristic adenine-nicotinamide interaction suggests that the coenzyme is bound in an unstacked conformation. 3. Glutarate and succinate, substrate analogues that are both inhibitors competitive with glutamate, do not significantly perturb the circular-dichroism spectrum of the enzyme in the absence of NAD+. 4. In the presence of NAD+, 150nM-succinate decreases the negative circular dichroism corresponding to bound coenzyme, but does not affect the protein circular dichroism. However, ISOmM-glutarate causes profound alternations of the circular-dichroism spectra of the bound NAD+ and of the enzyme, indicative of a protein conformational change. This direct evidence of conformational change specifically promoted by C5 dicarboxylates confirms the previous inference from protection studies. 5. The conformational change is discussed in relation to the allosteric mechanism of glutamate dehydrogenase.

Adenine binding to glutamate dehydrogenase: Natural and magnetic circular dichroism studies

FEBS Letters ◽  
1973 ◽  
Vol 31 (2) ◽  
pp. 251-255 ◽  
Author(s):  
J.M. Jallon ◽  
Y. Risler ◽  
C. Schneider ◽  
J.M. Thiery
Keyword(s):  
Circular Dichroism ◽  
Glutamate Dehydrogenase ◽  
Magnetic Circular Dichroism ◽  
Circular Dichroïsm

Characterization of Tamm-Horsfall Urinary Glycoprotein

1973 ◽  
Vol 31 ◽  
pp. 420-421
Author(s):  
John P. Robinson ◽  
J. David Puett
Keyword(s):  
Electron Microscopy ◽  
Circular Dichroism ◽  
Secondary Structure ◽  
Quaternary Structure ◽  
Normal Adult ◽  
Morphological Properties ◽  
Adult Males ◽  
Circular Dichroïsm ◽  
Urinary Glycoprotein

Much work has been reported on the chemical, physical and morphological properties of urinary Tamm-Horsfall glycoprotein (THG). Although it was once reported that cystic fibrotic (CF) individuals had a defective THG, more recent data indicate that THG and CF-THG are similar if not identical.No studies on the conformational aspects have been reported on this glycoprotein using circular dichroism (CD). We examined the secondary structure of THG and derivatives under various conditions and have correlated these results with quaternary structure using electron microscopy.THG was prepared from normal adult males and CF-THG from a 16-year old CF female by the method of Tamm and Horsfall. CF female by the method of Tamm and Horsfall.

Circular dichroism spectra of adsorbed dye-aggregates

1968 ◽  
Vol 65 ◽  
pp. 146-151 ◽  
Author(s):  
G. Scheibe ◽  
O. Wörz ◽  
F. Haimerl ◽  
W. Seiffert ◽  
J. Winkler
Keyword(s):  
Circular Dichroism ◽  
Circular Dichroism Spectra ◽  
Circular Dichroïsm
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