Affinity labeling of one of two α-neurotoxin binding sites in acetylcholine receptor from Torpedo californica

Biochemistry ◽  
1978 ◽  
Vol 17 (11) ◽  
pp. 2039-2045 ◽  
Author(s):  
Vinayak N. Damle ◽  
Arthur Karlin
Keyword(s):  
Acetylcholine Receptor ◽  
Binding Sites ◽  
Affinity Labeling ◽  
Torpedo Californica

Uses of fluorescent cholinergic analogs to study binding sites for cholinergic ligands in Torpedo californica acetylcholine receptor

Biochemistry ◽  
1979 ◽  
Vol 18 (10) ◽  
pp. 1855-1861 ◽  
Author(s):  
Jurgen Bode ◽  
Terry Moody ◽  
Michael Schimerlik ◽  
Michael Raftery
Keyword(s):  
Acetylcholine Receptor ◽  
Binding Sites ◽  
Torpedo Californica

Cholinergic binding sites on the pentameric acetylcholine receptor of Torpedo californica

Biochemistry ◽  
1993 ◽  
Vol 32 (33) ◽  
pp. 8608-8615 ◽  
Author(s):  
Susan M. J. Dunn ◽  
Michael A. Raftery
Keyword(s):  
Acetylcholine Receptor ◽  
Binding Sites ◽  
Torpedo Californica

m-[o-(2-Chloro-5-Fluorosulfonylphenylureido)Phenoxybutoxy]Benzamidine: Affinity Labeling Reagent Which Can Identify Secondary Binding Sites of Coagulation Complement and Fibrinolytic Serine Proteases

1979 ◽  
Author(s):  
D Bing ◽  
D Robison ◽  
J Andrews ◽  
R Laura
Keyword(s):  
Binding Sites ◽  
Serine Proteases ◽  
Enzyme Inhibitor ◽  
Molecular Model ◽  
Factor Xa ◽  
Affinity Labeling ◽  
Catalytic Center ◽  
Inhibitor Complex ◽  
Polypeptide Chains ◽  
Kinetics Of

We have determined that m-[o-(2-chloro-5-fluorosulfonylphenylureido)phenoxybutoxy]benza-midine [mCP(PBA)-F] is an affinity labeling reagent which labels both polypeptide chains of thrombin, factor Xa, complement component CIS and plasmin. As this means it is reacting outside of the catalytic center, we have called this reagent an exo-site affinity labeling reagent. Progressive irreversible inhibition of these enzymes by this reagent is rapid (k1st 2.5-4.6 x 10-3sec-1), the kinetics of inactivation are consistent with inhibition proceding via formation of a specific enzyme-inhibitor complex analogous to a Michaelis-Menton complex (KL - 115-26 μM), and diisopropylfluorophosphate or p-amidino-phenylmethanesulfonyfluoride Prevent labeling by [3H]mCP(PBA)-F. A molecular model of mCP(PBA)-F shows that the reactive SO2F group can be 17 A from the cationic amidine. The data are consistent with the hypothesis that both peptide chains are required for the specific proteolytic activity exhibited by these proteases and that the peptide chain which does not contain the active site serine is close to the catalytic center. (Supported by NIH and AHA grants

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