Fast NMR Methods for Measuring in the Direct and/or Competition Mode the Dissociation Constants of Chemical Fragments Interacting with a Receptor

ChemMedChem ◽  
2019 ◽  
Vol 14 (11) ◽  
pp. 1115-1127 ◽  
Author(s):  
Claudio Dalvit ◽  
Annick Parent ◽  
Francois Vallée ◽  
Magali Mathieu ◽  
Alexey Rak

Author(s):  
Abhinav Dubey ◽  
Shivanand M. Pudakalakatti ◽  
Hanudatta S. Atreya




2011 ◽  
Vol 51 (4) ◽  
pp. 487-495 ◽  
Author(s):  
François-Xavier Theillet ◽  
Andres Binolfi ◽  
Stamatis Liokatis ◽  
Silvia Verzini ◽  
Philipp Selenko


2017 ◽  
Vol 4 (1) ◽  
pp. 2 ◽  
Author(s):  
Bankala Krishnarjuna ◽  
Kousik Chandra ◽  
Hanudatta Atreya






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.



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


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