Binding modes of cibacron blue with albumin in affinity chromatography using docking tools

2021 ◽  
Vol 183 ◽  
pp. 110-118
Author(s):  
Seçkin Kılıç ◽  
Müge Andaç ◽  
Adil Denizli
Author(s):  
Hiroaki Ito ◽  
Hideo Yamamoto ◽  
Yoshihiro Kimura ◽  
Hiroshi Kambe ◽  
Toshikazu Okochi ◽  
...  

1988 ◽  
Vol 32 (4) ◽  
pp. 187-195
Author(s):  
Kiyotaka Fujita ◽  
Ikunosuke Sakurabayashi ◽  
Tadashi Kawai ◽  
Mutsuko Kusanagi ◽  
Yoshimi Teramura

1983 ◽  
Vol 130 (2) ◽  
pp. 481-484 ◽  
Author(s):  
Candadai S. Ramadoss ◽  
Janusz Steczko ◽  
John W. Uhlig ◽  
Bernard Axelrod

1981 ◽  
Vol 197 (1) ◽  
pp. 227-232 ◽  
Author(s):  
J Sobhanaditya ◽  
N A Rao

Flavokinase was purified, for the first time from a plant source [mung bean (Phaseolus aureus)] by affinity chromatography in the presence of orthophosphate and by using C-8 ATP-agarose (ATP linked through the C-8 position to beaded agarose), Cibacron Blue and riboflavin-Sepharoses. An altered substrates-saturation pattern was observed in the presence of K2HPO4. The conformational changes of the enzyme in the presence of K2HPO4 were monitored by fluorescence spectroscopy. These results highlight the regulatory nature of this enzyme.


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