Differential interactions of imatinib mesylate with the membrane skeletal protein spectrin and hemoglobin

RSC Advances ◽  
2016 ◽  
Vol 6 (60) ◽  
pp. 55203-55210 ◽  
Author(s):  
Debashree Das ◽  
Ushasi Pramanik ◽  
Malay Patra ◽  
Mousumi Banerjee ◽  
Abhijit Chakrabarti

The anti-leukaemia drug imatinib has been shown to bind to spectrin, and to hemoglobin in its oxy-form with binding dissociation constants of 48 μM and 63 μM at 25 °C respectively.

1984 ◽  
Vol 52 (03) ◽  
pp. 347-349 ◽  
Author(s):  
Daan W Traas ◽  
Bep Hoegee-de Nobel ◽  
Willem Nieuwenhuizen

SummaryNative human plasminogen, the proenzyme of plasmin (E. C. 3.4.21.7) occurs in blood in two well defined forms, affinity forms I and II. In this paper, the feasibility of separating these forms of human native plasminogen by affinity chromatography, is shown to be dependent on two factors: 1) the ionic composition of the buffer containing the displacing agent: buffers of varying contents of sodium, Tris, phosphate and chloride ions were compared, and 2) the type of adsorbent. Two adsorbents were compared: Sepharose-lysine and Sepharose-bisoxirane-lysine. Only in the phosphate containing buffers, irrespective of the type of adsorbent, the affinity forms can be separated. The influence of the adsorbent can be accounted for by a large difference in dissociation constants of the complex between plasminogen and the immobilized lysine.


2013 ◽  
Author(s):  
Berengere Gobin ◽  
Gatien Moriceau ◽  
Benjamin Ory ◽  
Regis Brion ◽  
Francoise Redini ◽  
...  
Keyword(s):  

2014 ◽  
Vol 2 (42) ◽  
pp. 263-263
Author(s):  
Farhoush Kiani ◽  
Mahmoud Tajbakhsh ◽  
Fereydoon Ashrafi ◽  
Nesa Shafiei ◽  
Azar Bahadori ◽  
...  

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