Thermodynamic descriptors, profiles and driving forces in membrane receptor-ligand interactions

2010 ◽  
Vol 30 (6) ◽  
pp. 454-468 ◽  
Author(s):  
Vladimir Pliska
Keyword(s):  
Driving Forces ◽  
Membrane Receptor ◽  
Receptor Ligand ◽  
Ligand Interactions

BirA Enzyme: Production and Application in the Study of Membrane Receptor–Ligand Interactions by Site-Specific Biotinylation

1999 ◽  
Vol 266 (1) ◽  
pp. 9-15 ◽  
Author(s):  
Christopher A. O'Callaghan ◽  
Michael F. Byford ◽  
Jessica R. Wyer ◽  
Benjamin E. Willcox ◽  
Bent K. Jakobsen ◽  
...  
Keyword(s):  
Enzyme Production ◽  
Membrane Receptor ◽  
Receptor Ligand ◽  
Site Specific ◽  
Ligand Interactions

Modulation of Platelet Activation by Native DNA – Initial Description of Platelet Receptor Type, Number and Discrimination for Native DNA

1981 ◽  
Vol 45 (03) ◽  
pp. 263-266 ◽  
Author(s):  
B A Fiedel ◽  
M E Frenzke
Keyword(s):  
Platelet Aggregation ◽  
Human Platelets ◽  
Scatchard Analysis ◽  
Type Number ◽  
Single Class ◽  
Receptor Ligand ◽  
Platelet Receptor ◽  
Platelet Binding ◽  
Ligand Interactions ◽  
Initial Description

SummaryNative DNA (dsDNA) induces the aggregation of isolated human platelets. Using isotopically labeled dsDNA (125I-dsDNA) and Scatchard analysis, a single class of platelet receptor was detected with a KD = 190 pM and numbering ~275/platelet. This receptor was discriminatory in that heat denatured dsDNA, poly A, poly C, poly C · I and poly C · poly I failed to substantially inhibit either the platelet binding of, or platelet aggregation induced by, dsDNA; by themselves, these polynucleotides were ineffective as platelet agonists. However, poly G, poly I and poly G · I effectively and competitively inhibited platelet binding of the radioligand, independently activated the platelet and when used at a sub-activating concentration decreased the extent of dsDNA stimulated platelet aggregation. These data depict a receptor on human platelets for dsDNA and perhaps certain additional polynucleotides and relate receptor-ligand interactions to a physiologic platelet function.

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