Evaluating dispersion in gel permeation chromatography. Axial dispersion of polymer molecules in packed beds of nonporous glass beads

1969 ◽  
Vol 41 (7) ◽  
pp. 874-879 ◽  
Author(s):  
R. N. Kelley ◽  
F. W. Billmeyer
Keyword(s):  
Gel Permeation Chromatography ◽  
Glass Beads ◽  
Axial Dispersion ◽  
Packed Beds ◽  
Polymer Molecules ◽  
Gel Permeation

On the dimensions of intramolecularly crosslinked polymer molecules - III. The measurement of the dimensions of intramolecularly crosslinked polystyrene

1973 ◽  
Vol 334 (1599) ◽  
pp. 477-491 ◽  
Keyword(s):  
Light Scattering ◽  
Molecular Mass ◽  
Mass Distribution ◽  
Molecular Mass Distribution ◽  
Gel Permeation Chromatography ◽  
Polymer Molecules ◽  
Crosslinked Polymer ◽  
Crosslinked Polystyrene ◽  
Gel Permeation ◽  
Molecular Masses

The intramolecularly crosslinked polystyrene molecules, prepared as in part I of this series, were examined by the techniques of light scattering, osmometry, viscometry, and gel permeation chromatography. Their molecular masses and molecular mass distribution remained constant over all the stages of the reaction radii of gyration were determined and the results compared with those predicted in part II of this series.

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.

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