Copolymer Analysis with Gel Permeation Chromatography: A Comparison of Methods Using Computerized IR Spectroscopy

1979 ◽  
Vol 17 (6) ◽  
pp. 336-339 ◽  
Author(s):  
E. G. Bartick
Keyword(s):  
Ir Spectroscopy ◽  
Gel Permeation Chromatography ◽  
Comparison Of Methods ◽  
Gel Permeation ◽  
Copolymer Analysis

Selective modification of polylactide by introducing acrylate groups: IR spectroscopy, gel permeation chromatography, and differential thermal analysis

2016 ◽  
Vol 90 (10) ◽  
pp. 1925-1930 ◽  
Author(s):  
V. T. Shashkova ◽  
I. A. Matveeva ◽  
N. N. Glagolev ◽  
T. S. Zarkhina ◽  
P. S. Timashev ◽  
...  
Keyword(s):  
Thermal Analysis ◽  
Differential Thermal Analysis ◽  
Ir Spectroscopy ◽  
Gel Permeation Chromatography ◽  
Gel Permeation

A Comparative Study of the Structure and Properties of Certain Types of Oligodiene

2018 ◽  
Vol 45 (1) ◽  
pp. 27-30
Author(s):  
N.A. Shabunina ◽  
V.D. Voronchikhin ◽  
E.I. Lesik ◽  
A.V. Berestyuk ◽  
O.V. Karmanova ◽  
...  
Keyword(s):  
Comparative Analysis ◽  
Ir Spectroscopy ◽  
Gel Permeation Chromatography ◽  
Molecular Characteristics ◽  
Structure And Properties ◽  
Gel Permeation ◽  
Temperature Dependences ◽  
Infrared Spectrometer ◽  
Processing Properties ◽  
Rotary Viscometer

Using methods of IR spectroscopy (Fourier infrared spectrometer; PerkinElmer) and gel permeation chromatography (Agilent 1200; Agilent Technologies), we studied the microstructure and molecular characteristics of four types of diene oligomer (DO) of different functionality. The dynamic viscosity, η, of DOs was measured on a rotary viscometer (LVDV-II + Pro; Brookfield). A comparative analysis of the obtained results makes it possible to predict the dispersion and the plasticising effect of DOs in polymer–oligomer composites. The temperature dependences of η for different DOs differ in the temperature range 20–60°C; at temperatures of 80°C and above, the values of h are practically identical, i.e. their processing properties are the same, and the replacement of one DO with another will not lead to any need to alter the processing regime of the composites.

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.

Gel Permeation Chromatography of Polyelectrolytes

1981 ◽  
Vol 4 (8) ◽  
pp. 1297-1309 ◽  
Author(s):  
M. Rinaudo ◽  
J. Desbrières ◽  
C. Rochas
Keyword(s):  
Gel Permeation Chromatography ◽  
Gel Permeation
Sign in / Sign up

Export Citation Format

Share Document