Specific affinity-labeling of the nociceptin ORL1 receptor using a thiol-activated Cys(Npys)-containing peptide ligand

Biopolymers ◽  
2016 ◽  
Vol 106 (4) ◽  
pp. 460-469 ◽  
Author(s):  
Ayami Matsushima ◽  
Hirokazu Nishimura ◽  
Yutaka Matsuyama ◽  
Xiaohui Liu ◽  
Tommaso Costa ◽  
...  
1995 ◽  
Vol 5 (15) ◽  
pp. 1609-1614 ◽  
Author(s):  
Takeshi Sagara ◽  
Mikako Okamura ◽  
Yasuyuki Shimohigashi ◽  
Motonori Ohno ◽  
Ken Kanematsu

1994 ◽  
Vol 67 (1) ◽  
pp. 296-299 ◽  
Author(s):  
Teruo Yasunaga ◽  
Yasuyuki Shimohigashi ◽  
Hiroaki Kodama ◽  
Masaya Miyazaki ◽  
Masaya Nagaishi ◽  
...  

1979 ◽  
Author(s):  
D Bing ◽  
D Robison ◽  
J Andrews ◽  
R Laura

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


2007 ◽  
Vol 27 (4) ◽  
pp. 345-356 ◽  
Author(s):  
Linda K. Myers ◽  
Bo Tang ◽  
Edward F. Rosioniec ◽  
John M. Stuart ◽  
Andrew H. Kang

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