31P NMR studies of the ATP/α-crystallin complex: Functional implications

31P NMR studies of the ATP/α-crystallin complex: Functional implications

Evidence is presented for the binding of ATP to α-crystallin in the lens by 31P NMR spectroscopic measurements. The chemical shift data as well as the T 1 and T 2 values indicate that P β and P γ of ATP are of prime importance in binding. In addition, it is demonstrated that the association of α-cry...

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Veröffentlicht in:Biochemical and biophysical research communications 1992-12, Vol.189 (3), p.1578-1584
Hauptverfasser: Reddy, M.C., Palmisano, D.V., Groth-Vasselli, B., Farnsworth, P.N.
Format: Artikel
Sprache:eng
Schlagworte:
Adenosine Triphosphate - chemistry
Adenosine Triphosphate - metabolism
Animals
Biological and medical sciences
Cattle
Crystallins - chemistry
Crystallins - isolation & purification
Crystallins - metabolism
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
Interactions. Associations
Intermolecular phenomena
Magnetic Resonance Spectroscopy - methods
Molecular biophysics
Phosphorus
Protein Conformation
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Zusammenfassung:Evidence is presented for the binding of ATP to α-crystallin in the lens by 31P NMR spectroscopic measurements. The chemical shift data as well as the T 1 and T 2 values indicate that P β and P γ of ATP are of prime importance in binding. In addition, it is demonstrated that the association of α-crystallin with purified fiber cell membranes is significantly enhanced by the addition of ATP. These results suggest that ATP modulates the functional behavior of α-crystallin.
ISSN:0006-291X
1090-2104
DOI:10.1016/0006-291X(92)90256-K