Interaction of the cysteine proteinase inhibitor chicken cystatin with papain

Biochemistry ◽  
1988 ◽  
Vol 27 (14) ◽  
pp. 5074-5082 ◽  
Author(s):  
Peter Lindahl ◽  
Eva Alriksson ◽  
Hans Jörnvall ◽  
Ingemar Bjoerk
FEBS Letters ◽  
1989 ◽  
Vol 248 (1-2) ◽  
pp. 162-168 ◽  
Author(s):  
Bernd Laber ◽  
Kerstin Krieglstein ◽  
Agnes Henschen ◽  
Janko Kos ◽  
Vito Turk ◽  
...  

1990 ◽  
Vol 271 (1) ◽  
pp. 281-284 ◽  
Author(s):  
M Nycander ◽  
I Björk

The single tryptophan residue Trp-104 of chicken cystatin was modified with a 2-hydroxy-5-nitrobenzyl group. The change of the absorption spectrum of this group on binding of the modified cystatin to papain indicated a decreased environmental polarity of the probe. The modified inhibitor had about a 10(5)-fold lower affinity for papain than had intact cystatin, this being due to a higher dissociation rate constant. These results show that Trp-104 of cystatin is located in or near the proteinase-binding site of the inhibitor, in agreement with a model proposed from computer docking Experiments.


1986 ◽  
Vol 236 (1) ◽  
pp. 312-312 ◽  
Author(s):  
A J Barrett ◽  
H Fritz ◽  
A Grubb ◽  
S Isemura ◽  
M Järvinen ◽  
...  

2021 ◽  
Vol 25 ◽  
pp. 100876
Author(s):  
Natalia N.S. Nunes ◽  
Rodrigo S. Ferreira ◽  
Leonardo F.R. de Sá ◽  
Antônia Elenir A. de Oliveira ◽  
Maria Luiza V. Oliva

1985 ◽  
Vol 49 (3) ◽  
pp. 799-805
Author(s):  
Kyoichi Ogura ◽  
Mitsuru Maeda ◽  
Masami Nagai ◽  
Takaharu Tanaka ◽  
Kyosuke Nomoto ◽  
...  

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