31P NMR studies of the ATP/alpha-crystallin complex: functional implications.
Evidence is presented for the binding of ATP to alpha-crystallin in the lens by 31P NMR spectroscopic measurements. The chemical shift data as well as the T1 and T2 values indicate that P beta and P gamma of ATP are of prime importance in binding. In addition, it is demonstrated that the association of alpha-crystallin with purified fiber cell membranes is significantly enhanced by the addition of ATP. These results suggest that ATP modulates the functional behavior of alpha-crystallin.
Reddy
M C
MC
Department of Physiology, UMD-New Jersey Medical School, Newark 07103.
Palmisano
D V
DV
Groth-Vasselli
B
B
Farnsworth
P N
PN
D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D003459:Crystallins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D010758:Phosphorus; D011487:Protein Conformation
D003459:Crystallins; D010758:Phosphorus; D000255:Adenosine Triphosphate