Identification of the tRNA-binding sites on rat liver ribosomes by affinity labeling

1977 ◽  
Vol 153 (3) ◽  
pp. 231-235 ◽  
Author(s):  
A. Peter Czernilofsky ◽  
Ekkehard Collatz ◽  
Axel M. Gressner ◽  
Ira G. Wool ◽  
Ernst Küchler
1981 ◽  
Vol 184 (3) ◽  
pp. 551-556 ◽  
Author(s):  
Steven Fabijanski ◽  
Maria Pellegrini

Biochemistry ◽  
1997 ◽  
Vol 36 (34) ◽  
pp. 10492-10497 ◽  
Author(s):  
Anna V. El'skaya ◽  
Galina V. Ovcharenko ◽  
Sergey S. Palchevskii ◽  
Zoja M. Petrushenko ◽  
Francisco J. Triana-Alonso ◽  
...  

Author(s):  
James Ofengand ◽  
Robert Denman ◽  
Kelvin Nurse ◽  
Arnold Liebman ◽  
David Malarek ◽  
...  

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


1965 ◽  
Vol 240 (7) ◽  
pp. 3009-3015 ◽  
Author(s):  
William A. Warren ◽  
Theodore Peters
Keyword(s):  

1980 ◽  
Vol 255 (14) ◽  
pp. 6954-6961 ◽  
Author(s):  
A.M. Reboud ◽  
S. Dubost ◽  
M. Buisson ◽  
J.P. Reboud

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