Prevention of Molecular Self-Association by Sodium Salicylate: Effect on Insulin and 6-Carboxyfluorescein

1987 ◽  
Vol 76 (10) ◽  
pp. 791-793 ◽  
Author(s):  
E. Touitou ◽  
F. Alhaique ◽  
P. Fisher ◽  
A. Memoli ◽  
F.M. Riccieri ◽  
...  
Keyword(s):  
Sodium Salicylate ◽  
Self Association

Self association of sodium salicylate system

2003 ◽  
Vol 293 (2) ◽  
pp. 211-216 ◽  
Author(s):  
Subir Kumar Das ◽  
Shrabani Das ◽  
B.Nandi Ganguly ◽  
Amarnath Maitra
Keyword(s):  
Sodium Salicylate ◽  
Self Association

Aggregated, Conformationally Changed Fibrinogen Exposes the Stimulating Sites for t-PA-Catalysed Plasminogen Activation

1996 ◽  
Vol 75 (02) ◽  
pp. 326-331 ◽  
Author(s):  
Unni Haddeland ◽  
Knut Sletten ◽  
Anne Bennick ◽  
Willem Nieuwenhuizen ◽  
Frank Brosstad
Keyword(s):  
Conformational Changes ◽  
Gel Permeation Chromatography ◽  
Tissue Type ◽  
Plasminogen Activation ◽  
Chromogenic Substrate ◽  
Type Plasminogen Activator ◽  
Gel Permeation ◽  
Self Association ◽  
Fibrin Monomers ◽  
Stimulation Of

SummaryThe present paper shows that conformationally changed fibrinogen can expose the sites Aα-(148-160) and γ-(312-324) involved in stimulation of the tissue-type plasminogen activator (t-PA)-catalysed plasminogen activation. The exposure of the stimulating sites was determined by ELISA using mABs directed to these sites, and was shown to coincide with stimulation of t-PA-catalysed plasminogen activation as assessed in an assay using a chromogenic substrate for plasmin. Gel permeation chromatography of fibrinogen conformationally changed by heat (46.5° C for 25 min) demonstrated the presence of both aggregated and monomeric fibrinogen. The aggregated fibrinogen, but not the monomeric fibrinogen, had exposed the epitopes Aα-(148-160) and γ-(312-324) involved in t-PA-stimulation. Fibrinogen subjected to heat in the presence of 3 mM of the tetrapeptide GPRP neither aggregates nor exposes the rate-enhancing sites. Thus, aggregation and exposure of t-PA-stimulating sites in fibrinogen seem to be related phenomena, and it is tempting to believe that the exposure of stimulating sites is a consequence of the conformational changes that occur during aggregation, or self-association. Fibrin monomers kept in a monomeric state by a final GPRP concentration of 3 mM do not expose the epitopes Aα-(148-160) and γ-(312-324) involved in t-PA-stimulation, whereas dilution of GPRP to a concentration that is no longer anti-polymerizing, results in exposure of these sites. Consequently, the exposure of t-PA-stimulating sites in fibrin as well is due to the conformational changes that occur during selfassociation.

Self-association of insulin. Its pH dependence and effect of plasma

Diabetes ◽  
1987 ◽  
Vol 36 (3) ◽  
pp. 261-264 ◽  
Author(s):  
E. Helmerhorst ◽  
G. B. Stokes
Keyword(s):  
Ph Dependence ◽  
Self Association

Understanding Self-Association and Tubule Formation in Phytosterol-Based Oleogels

2020 ◽  
Author(s):  
Stephen Euston ◽  
Paul Clegg ◽  
George Dalkas ◽  
Andrew Matheson
Keyword(s):  
Tubule Formation ◽  
Self Association
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