Thin-layer gel permeation chromatography: a technique to separate molecules according to molecular size

1983 ◽  
Vol 60 (5) ◽  
pp. 430 ◽  
Author(s):  
Neil J. Moir
Keyword(s):  
Thin Layer ◽  
Molecular Size ◽  
Gel Permeation Chromatography ◽  
Gel Permeation

scholarly journals Correlations between retention volume and molecular size parameters in gel permeation chromatography of small molecules

1975 ◽  
Vol 28 (1) ◽  
pp. 189 ◽  
Author(s):  
RA Shanks
Keyword(s):  
Molecular Weight ◽  
Small Molecules ◽  
Organic Molecules ◽  
Retention Volume ◽  
Molecular Size ◽  
Gel Permeation Chromatography ◽  
Molar Volumes ◽  
Small Organic Molecules ◽  
Molecular Dimension ◽  
Gel Permeation

Gel permeation columns of Bio Beads S-X8 have been used to provide separation of oligomers and other small organic molecules. Results show successful separations up to molecular weight c. 600. The retention times of compounds have been correlated with the largest molecular dimension of the molecules and also with molar volumes.

scholarly journals Fucose content of keratan sulphates from bovine articular cartilage

1991 ◽  
Vol 273 (2) ◽  
pp. 307-310 ◽  
Author(s):  
G H Tai ◽  
G M Brown ◽  
H G Morris ◽  
T N Huckerby ◽  
I A Nieduszynski
Keyword(s):  
Molecular Weight ◽  
Articular Cartilage ◽  
Molecular Size ◽  
Gel Permeation Chromatography ◽  
Repeat Sequence ◽  
Keratan Sulphate ◽  
Bovine Articular Cartilage ◽  
Gel Permeation ◽  
Fucose Content ◽  
Galactose Content

Alkaline-borohydride-reduced keratan sulphate chains were isolated from bovine articular cartilage (6-8-year-old animals). Nine keratan sulphate fractions of increasing molecular weight were prepared by gel-permeation chromatography on a calibrated column of TSK 30 XL. The samples were analysed for fucose and galactose contents (% by wt. of keratan sulphate) and fucose/galactose ratio. The fucose content increased with molecular size, but the galactose content remained constant. It was concluded that the alpha(1→3)-linked fucose [Thornton, Morris, Cockin, Huckerby, Nieduszynski, Carlstedt, Hardingham & Ratcliffe (1989) Biochem. J. 260, 277-282] was located within the poly-N-acetyl-lactosamine repeat sequence of articular-cartilage keratan sulphate.

Molecular Size of the Diapause Hormone of the Silkworm Bombyx mori

1976 ◽  
Vol 31 (3-4) ◽  
pp. 132-134 ◽  
Author(s):  
Ichiro Kubota ◽  
Minoru Isobe ◽  
Toshio Goto ◽  
Kinsaku Hasegawa
Keyword(s):  
Molecular Weight ◽  
Bombyx Mori ◽  
Organic Solvents ◽  
Molecular Size ◽  
Gel Permeation Chromatography ◽  
Molecular Weights ◽  
Gel Permeation ◽  
Modified Peptides ◽  
Diapause Hormone ◽  
Silkworm Bombyx Mori

Abstract The diapause hormone (D H) responsible for arrested development of the silkworm Bombix mori consists of two active principles of peptide (A and B) . Since both hormones form aggregates in aqueous phases, the molecular weights were determined by gel permeation chromatography of Merckogel OR 6000 using methanol-dichloromethane mixture as the developing agent. Gramicidins and modified peptides soluble in the organic solvents were used as the standard markers for the molecular weight measurements of the hormones. The molecular weights of DH -A and -B are estimated to be 3300 ± 400 and 2000 ± 200, respectively.

High Molecular Weight Complexes Derived From Fibrinogen

1981 ◽  
Author(s):  
N Alkjaersig ◽  
A Fletcher
Keyword(s):  
Molecular Weight ◽  
Complex Formation ◽  
High Molecular Weight ◽  
Molecular Size ◽  
Gel Permeation Chromatography ◽  
Linear Increase ◽  
Clot Formation ◽  
High Molecular Weight Complex ◽  
Fibrin Monomer ◽  
Gel Permeation

Fibrinogen, 3×10-5 M, incubated at 25°C with thrombin 10-10 M, is slowly transformed to fibrin. Fibrinopeptide A (FPA) is released at a rate of approximately 1 nM/ml per min, and after 30 min a clot is formed. Prior to clot formation serially timed solution aliquots were examined by gel permeation chromatography on a Bio Gel 5M column (void volume 140 ml). High molecular weight complex concentration and molecular size increased with incubation time. Fibrinogen antigen and FPA concentration was determined for each effluent fraction and relative FPA content (ng FPA/μg fibrinogen equivalent) was linearly related to chromatographic effluent volume between 160 and 260 ml (Ve for fibrinogen 255 ml). Computer analysis of the effluent profiles indicated a linear fall in monomeric fibrinogen to 20% of original concentration, a linear increase in “fibrin” dimer (2 fibrinogen equivalents with 2 FPA) to 30% and in trimer (3 fibrinogen equivalents with 2 FPA) to 20% of original concentration with higher polymers accounting for the remaining protein. These complexes were stable and remained in solution after fractionation. Fibrin monomer, in 3 M urea and devoid of FPA, when added to fibrinogen resulted in clot formation, equivalent to 66% of added monomer, but minimal complex formation, 5% of total fibrinogen equivalents. Thus intermediate fibrin polymers which contain residual FPA are stable soluble molecular entities in contradistinction to fibrin monomer lacking FPA. Fibrin proteolysis products added to fibrinogen also show minimal complex formation with fibrinogen if the products are free of thrombin and FPA. Patient plasma samples can be similarly assayed and distinction can be made between high molecular weight complexes derived from fibrinogen through thrombin action or from fibrin through plasmin action.

scholarly journals Formation of soluble fibrin oligomers in purified systems and in plasma

1983 ◽  
Vol 213 (1) ◽  
pp. 75-83 ◽  
Author(s):  
N Alkjaersig ◽  
A P Fletcher
Keyword(s):  
Sol Gel ◽  
Molecular Size ◽  
Gel Permeation Chromatography ◽  
Fibrinopeptide A ◽  
Human Fibrinogen ◽  
Soluble Polymers ◽  
Polymer Formation ◽  
Gel Permeation ◽  
Sol Gel Transition ◽  
Gel Transition

The kinetic parameters for release of fibrinopeptide A (FPA) from human fibrinogen by thrombin are: Km = 2.3 × 10(-6)M and Vmax. = 1.1 × 10(-10)mol of FPA/s per unit of thrombin; for fibrin formation, Km is similar to that for FPA release, but, the conditions of the present study, Vmax. was approximately half of that for FPA release. The formation of fibrin polymer before the sol-gel transition was studied by gel-permeation chromatography combined with effluent analysis for fibrinogen antigen and residual FPA. Polymer formation in purified fibrinogen incubated with thrombin proceeded as a bimolecular association of exposed sites in a manner predicted by probability calculations and assuming random FPA cleavage. Each oligomer consisted of n molecules of fibrin monomer and two fibrinogen molecules, each of the latter lacking one FPA molecule, i.e. each oligomer, regardless of molecular size, retains two FPA molecules. The addition of 5 mM-CaCl2 to the reaction mixture changed the rate of polymer formation, so that dimer was no longer the prevalent oligomer; in the presence of Ca2+, the trimer was the oligomer in highest concentration. The polymers formed in the presence of calcium were similar in composition to those without, i.e. 2 mol of FPA/mol of oligomer. EDTA-treated plasma samples incubated for short periods of time, 30s or less, with thrombin ranging in concentration up to 1 N.I.H. unit/ml did not form clots during the 10-15 min period of observation until they were applied to the column, though a large proportion of the available FPA was cleaved (maximum 45%). The soluble polymers in plasma were mostly of the high-Mr variety (tetramer and greater); these high-Mr polymers contained less than 2 mol of FPA/mol of polymer, whereas dimer and trimer in plasma were similar to those in the purified systems, i.e. 2 mol of FPA/mol.

Gel Permeation Chromatography of Heparins

1980 ◽  
Vol 43 (03) ◽  
pp. 192-193 ◽  
Author(s):  
Barbara Mulloy ◽  
Edward A Johnson
Keyword(s):  
Biological Activity ◽  
Molecular Size ◽  
Gel Permeation Chromatography ◽  
Biological Investigation ◽  
Water As Solvent ◽  
Gel Permeation ◽  
Heparin Fractions

SummaryGel permeation chromatography of heparins using water as solvent has recently been used to obtain fractions for biological investigation. We find that heparin fractions obtained in this way are not, necessarily, differentiated simply on a molecular size basis as has been alleged. Correlations between biological activity and molecular size obtained using such fractions must therefore be treated with caution.

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