Correction for axial dispersion in gel permeation chromatography with a detector of molecular masses

1982 ◽  
Vol 7 (11-12) ◽  
Author(s):  
Milo? Netopil�k
Keyword(s):  
Gel Permeation Chromatography ◽  
Axial Dispersion ◽  
Gel Permeation ◽  
Molecular Masses

Detection of serum proteins by high-pressure gel-permeation chromatography with low-angle laser light scattering, compared with analytical ultracentrifugation.

1986 ◽  
Vol 32 (2) ◽  
pp. 363-367 ◽  
Author(s):  
W Flapper ◽  
P J van den Oetelaar ◽  
C P Breed ◽  
J Steenbergen ◽  
H J Hoenders
Keyword(s):  
High Pressure ◽  
Light Scattering ◽  
Analytical Ultracentrifugation ◽  
Laser Light ◽  
Serum Proteins ◽  
Gel Permeation Chromatography ◽  
Laser Light Scattering ◽  
Gel Permeation ◽  
Human Sera ◽  
Molecular Masses

Abstract Human sera were subjected to analytical ultracentrifugation and "high-pressure" gel-permeation chromatography on a system of combined TSK Gel G5000 PW and G3000 SW columns. The chromatographic method produced remarkably superior resolution of the proteins, especially those exceeding 100 000 Da. We calculated the molecular masses of eluted fractions on the basis of their detection by low-angle laser light scattering and their differential refractive index. We discuss the results in relation to the clinical data.

Determination of the molecular masses of tetrafluoroethylene telomers by gel-permeation chromatography

2009 ◽  
Vol 51 (7) ◽  
pp. 785-790 ◽  
Author(s):  
A. I. Kuzaev ◽  
I. P. Kim ◽  
D. P. Kiryukhin ◽  
V. M. Buznik
Keyword(s):  
Gel Permeation Chromatography ◽  
Gel Permeation ◽  
Molecular Masses

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.

Serum Catalase: Reversibly Formed Charge Isoform of Erythrocyte Catalase

1991 ◽  
Vol 37 (12) ◽  
pp. 2043-2047 ◽  
Author(s):  
László Góth
Keyword(s):  
Electrophoretic Mobility ◽  
Serum Proteins ◽  
Binding Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Permeation Chromatography ◽  
Electrophoretic Mobilities ◽  
Erythrocyte Catalase ◽  
Gel Permeation ◽  
Human Sera ◽  
Molecular Masses

Abstract The different electrophoretic mobilities of erythrocyte and serum catalase (EC 1.11.1.6) were confirmed and the causes responsible for their differences were examined. The presence of a catalase-binding protein in serum that could form a complex with erythrocyte catalase was excluded by incubating serum proteins with erythrocyte catalase. No new unequivocal catalase bands representing a catalase-binding protein were detected. The erythrocyte and serum catalase proved to be charge isoforms: their molecular masses, estimated by gel permeation chromatography or polyacrylamide gel electrophoresis in a nondenaturing system, were very similar, whereas their electrophoretic mobilities were different. Assay of serum catalase by gel permeation and hydrophobic chromatography yielded a product with the same electrophoretic mobility as that of erythrocyte catalase. Different dilution of erythrocyte catalase with human sera led to a gradual decrease of its mobility, 20-fold or greater dilution yielding the same results as for serum catalase. Similarly, when serum catalase was diluted 20-fold or more with 60 mmol/L phosphate buffer, it migrated similarly to erythrocyte catalase. I detected no effect of dialyzable serum ligands, NADPH, or protection of SH groups on the electrophoretic mobility of either catalase isoform. I conclude that formation of charge isoforms of catalase is caused by a reversible, conformational modification due to matrix effect of serum.

Chitinases of Bacillus licheniformis B-6839: isolation and properties

1996 ◽  
Vol 42 (4) ◽  
pp. 307-315 ◽  
Author(s):  
Lesya A. Trachuk ◽  
Lyudmila P. Revina ◽  
Tatyana M. Shemyakina ◽  
Galina G. Chestukhina ◽  
Valentin M. Stepanov
Keyword(s):  
Ion Exchange ◽  
Bacillus Licheniformis ◽  
Gel Permeation Chromatography ◽  
The Other ◽  
Colloidal Chitin ◽  
Bacillus Circulans ◽  
Temperature Optimum ◽  
Chitinase A ◽  
Gel Permeation ◽  
Molecular Masses

Five chitinases were isolated from culture filtrates of Bacillus licheniformis B-6839 R and S variants by combination of hydrophobic, ion-exchange, and gel permeation chromatography. The enzymes had molecular masses of 66, 62, 53, 49, and 42 kDa. The chitinases revealed two activity optima against colloidal chitin at pH 4.5–5.5 and 9.0–9.5 and they were rather stable at pH 4.0–9.5. The temperature optimum of activity was 90 °C for the 62-kDa chitinase and 70 °C for the other enzymes. The 66-, 53-, and 42-kDa chitinases showed pronounced similarities in their N-terminal sequences and apparently belonged to the same group, which might be related to Bacillus circulans chitinase A1. The 49- and 62-kDa enzymes did not reveal structural similarities with other chitinases produced by the studied B. licheniformis strain. No relationship was found with the 89- and 76-kDa chitinases isolated earlier from B. licheniformis X-7u.Key words: Bacillus licheniformis, chitinase, multiplicity.

Insulin-like growth factors I and II in healthy man.

1989 ◽  
Vol 121 (6) ◽  
pp. 753-758 ◽  
Author(s):  
Hans-Peter Guler ◽  
Jürgen Zapf ◽  
Christoph Schmid ◽  
E. Rudolf Froesch
Keyword(s):  
Protein Complexes ◽  
Gel Permeation Chromatography ◽  
Free Form ◽  
Carrier Protein ◽  
Recombinant Human Insulin ◽  
Gel Permeation ◽  
Igf I ◽  
Molecular Masses ◽  
Normal Adults ◽  
Insulin Like Growth Factors

Abstract. IGF-I and -II share specific serum carrier proteins which elute on neutral Sephadex G-200 gel permeation chromatography at apparent molecular masses of 50 and 200 kD. The half-lives of free and carrier protein-bound 125I-IGF-I and -II were determined after bolus injections of the tracers into two normal adults. Labelled IGF-I and -II migrated first with the 50-kD and later with the 200-kD complex. In these complexes their apparent half-lives were 20–30 min and 12–15 h, respectively. The apparent half-life of free 125I-IGF-I and -II was 10–12 min. In a second set of experiments, recombinant human insulin-like growth factor I was infused during 6 days in two healthy adults at a dose of 20 μg · kg−1 · h−1 (corresponding to around 30 mg/day). Serum obtained before and during the infusion was subjected to neutral Sephadex G-200 gel permeation chromatography and fractions were pooled according to the apparent molecular masses at which the carrier protein complexes elute. IGF-I and -II in these pools were determined by RIA. Before the IGF-I infusion, 92 and 272 μg/l of IGF-I and -II were found in the 200-kD complex, 45 and 91 μg/l in the 50-kD complex, and 15 and 5 μg/l were present in the free form. Corresponding figures during the IGF-I infusion were 389 and 18 μg/l for the 200-Kd complex, 201 and 54 μg/l for the 50-kD complex, and 80 and < 1 μg/l for free IGF-I and -II. Using the half-lives of the tracer studies and the levels of the different molecular weight forms of IGF in serum, the production rates for IGF-I and -II were calculated to be 10 mg and 13 mg per day.

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