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Results for “Chromatography, Gel”

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At least 19 recordsLinked to original sources
PubMed1978

An osmotic effect operative in frontal gel chromatography.

The osmotic effect operative in frontal gel chromatography was quantitatively studied. When mixtures of a non-penetrating solute (Kav = 0) and a partially penetrating solute (0 less than Kav less than 1) were subjected to frontal gel chromatography, the latter formed a coextensive concentration gradient across the trailing boundary of the former, leading to the formation of a second plateau where the concentration exceeded that of the original solution plateau. It was shown that this anomaly, which we have previously predicted, was a direct consequence of osmotic perturbation of the bead size of the Sephadex gel and could be satisfactorily described by an equation based solely on the osmotic distention of the gel beads. Finally, the implications of the osmotic effect in the frontal chromatographic analysis of acceptor-ligand interactions is discussed and a method for correcting this effect is presented.

Chromatography, Gel↗
PubMedDate not supplied

[Studies in heterogeneity of thymus lymphocytotropic low-molecular preparation by gel chromatography on Sephadex G-10].

The low-molecular thymus preparation obtained by dialysis and acetone precipitation is studied by gel chromatography on Sephadex G-10. Gel chromatography was performed on the column equilibrated with 6 M urea at pH 3. The column is calibrated with NADP, ATP, sucrose, glucose and KH2-PO4. The preparation was divided into two fractions with approximate molecular weights of 120-200 and 500-700 daltons.

Chromatography, Gel↗
PubMed1979

Gel chromatography applied to quantitation of components of IgG preparations.

Investigations were undertaken to standardize gel chromatography for quality control of IgG preparations. Great importance was attached to convenience of procedure. With application of the optimal type ofgel, Ultrogel AcA 34, the influence on quality of separation of various experimental parameters such as pH and ionic strength of the eluant, volume and concentration of the sample, flow rate and direction, and temperature were tested. Various methods of evaluation were applied. According to the demands, quantitation of components may be performed by collection of fractions and determination of peak volumes and protein concentrations, by determination of peak areas on absorbance recordings, or automatically by use of an integrator or a computer. The results obtained by gel chromatography are discussed and compared with the results of analytical ultracentrifugation.

Chromatography, Gel↗
PubMed1975

Fractionation of horseradish peroxidase by preparative isoelectric focusing, gel chromatography and ion-exchange chromatography.

Horseradish peroxidase has been fractionated by preparative isoelectric focusing in a density gradient and in a layer of granulated gel using pH-3-10 and narrow-pH-range carrier ampholytes at different total enzyme loads. The resolution of peroxidase isoenzymes in preparative-layer isoelectric focusing was comparable to that obtained by analytical thin-layer isoelectric focusing. Isoelectrically homogeneous isoenzymes could be isolated with good recovery in a single fractionation step. Despite the excellent separation of the individual isoenzymes by isoelectric focusing in gel layers, an effective purification, indicated by the absorbance ratio A403mn/A278nm, could not be achieved by focusing applied as a single step. By different fractionation sequences combining gel chromatography, ion-exchange chromatography, and isoelectric focusing, individual isoenzymes with a high purity and homogeneous with respect to their size and charge properties have been isolated.

Chromatography, Gel↗
PubMed1978

Characterization of bacterial L-(-)-tyrosine decarboxylase by isoelectric focusing and gel chromatography.

The purification of L-(-)-tyrosine apodecarboxylase (TAD) (E.C. 4.1.1.25), obtained from extracts of cells of Streptococcus faecalis, has been investigated by means of preparative isoelectric focusing, molecular sieve chromatography and hydrophobic interaction chromatography. Isoelectric focusing demonstrated two separate fractions possessing enzyme activity that had pI values of 4.5 and ca. 3.2. In the chromatographic methods, however, the activity was obtained in a single peak. It was found that hydrophobic interaction chromatography on phenyl-Sepharose was particularly suitable for purification purposes. The enzyme is very firmly bound to octyl-Sepharose CL-4B but retains most of its activity even in the bound state.

Chromatography, Gel↗
PubMed1979

Correlation of extracts obtained by high efficiency gel chromatography of lactic dehydrogenase virus infected mouse serum and cytosol from human tumors using leukocyte adherence inhibition assay.

Immunochemically active fractions were obtained using Separon Hema-300-glc(R) from serum of lactic dehydrogenase virus (LDV) infected mice and from homogenates of human tumors. The mixture of proteins of tumorous origin from the cytosol giving a positive reaction in the leukocyte adherence inhibition (LAI) test was found in the same fractions showing maximum of absorbance at 340 nm in the spectrophotometer and a corresponding peak in the refractometer. Analogous peaks were not proved in material obtained from healthy controls, but they were found in some human placentas and fetal organs. The LDV fraction obtained from mouse serum served as a "control" antigen in LAI test for human tumor testing, and results corresponded with those obtained using cytosol specific for the tumor under study.

Animals↗