title: 31P NMR studies of the ATP/alpha-crystallin complex: functional implications.
abstract: 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.
authors: Department of Physiology, UMD-New Jersey Medical School, Newark 07103.
authors: M C
authors: MC
authors: Reddy
authors: D V
authors: DV
authors: Palmisano
authors: B
authors: B
authors: Groth-Vasselli
authors: P N
authors: PN
authors: Farnsworth
mesh_terms: 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
chemical_list: D003459:Crystallins; D010758:Phosphorus; D000255:Adenosine Triphosphate