Stopped flow kinetics of carbamylcholine binding to membrane bound acetylcholine receptor

1978 ◽  
Vol 81 (3) ◽  
pp. 955-964 ◽  
Author(s):  
U. Quast ◽  
M. Schimerlik ◽  
M.A. Raftery
1987 ◽  
Vol 243 (1) ◽  
pp. 79-86 ◽  
Author(s):  
S R Patanjali ◽  
M J Swamy ◽  
A Surolia

The presence of two essential tryptophan residues/molecule was implicated in the binding site of Abrus agglutinin [Patanjali, Swamy, Anantharam, Khan & Surolia (1984) Biochem. J. 217, 773-781]. A detailed study of the stopped-flow kinetics of the oxidation of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues into two phases was observed upon ligand binding. The heterogeneity of tryptophan exposure was substantiated by quenching studies with acrylamide, succinimide and Cs+. Our study revealed the microenvironment of tryptophan residues to be hydrophobic, and also the presence of acidic amino acid residues in the vicinity of surface-localized tryptophan residues.


Biochemistry ◽  
1984 ◽  
Vol 23 (9) ◽  
pp. 2049-2056 ◽  
Author(s):  
Finn B. Hansen ◽  
Robert W. Noble ◽  
Murray J. Ettinger

1978 ◽  
Vol 100 (19) ◽  
pp. 6162-6166 ◽  
Author(s):  
Tadashi Okuyama ◽  
Yoshiya Ikenouchi ◽  
Takayuki Fueno

Biochemistry ◽  
1978 ◽  
Vol 17 (9) ◽  
pp. 1675-1682 ◽  
Author(s):  
Ulrich Quast ◽  
Juergen Engel ◽  
Erna Steffen ◽  
Harald Tschesche ◽  
Sigrid Kupfer

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