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Gel filtration chromatography,

Gel filtration chromatography on a Sephadex G 100 column has been used to fractionate humic acid. [Pg.11]


Gel permeation chromatography, exclusion chromatography. gel filtration chromatography. A technique for separating the components of a mixture according to molecular volume differences. A porous solid phase (a polymer, molecular sieve) is used which can physically entrap small molecules in the pores whilst large molecules pass down the column more rapidly. A solvent pressure up to 1000 psi may be used. [Pg.98]

Gel filtration chromatography (GFC) is the name used to describe this method of separation in the biochemical literature. Under this heading, the method is primarily applied to aqueous solutions of solutes of biological origin. [Pg.642]

W.W. Yau, D.D. By and J.J. Kirkland, Modern Size Exclusion Liquid Chromatography Practice of Gel Permeation and Gel Filtration Chromatography, J. Wiley and Sons, New York, 1979. ISBN 0471033871. [Pg.48]

EC 1.15.1.1]. Purified by DEAE-Sepharose and copper chelate affinity chromatography. The preparation was homogeneous by SDS-PAGE, analytical gel filtration chromatography and by isoelectric focusing [Weselake et al. Anal Biochem 155 193 1986 Fridovich J Biol Chem 244 6049 7969]. [Pg.523]

I. SILICA-BASED TSK-GEL SW/SWxl COLUMNS FOR GEL-FILTRATION CHROMATOGRAPHY (GFC)... [Pg.93]

TABLE 4.11 Recommended Column Selection Guide for High-Performance Gel-Filtration Chromatography... [Pg.132]

Sasaki, H., Natsuda, T., Ishikawa, O., Takamatsu, T., Tanaka, K., Kato, Y., and Hashimoto, T. (1985). New Series of TSK-GELPWType for High Performance Gel Filtration Chromatography. Scientific Report of Toyo Soda, 29(1). [Pg.529]

A new protein of unknown structure has been purified. Gel filtration chromatography reveals that the native protein has a molecular weight of 240,000. Chromatography in the presence of 6 M guanidine hydrochloride yields only a peak for a protein of M, 60,000. Chromatography in the presence of 6 M guanidine hydrochloride and 10 mM /3-mercaptoethanol yields peaks for proteins of M, 34,000 and 26,000. Explain what can be determined about the structure of this protein from these data. [Pg.207]

Although the total content of carbohydrate fractions of the three components is similar, as reported by Williams et al., 1990, it was found that protein-rich fractions have a significantly lower glucuronic acid content. Circular dichroism studies conducted on different GA fractions showed that only the AGP and GP components have a secondary structure (Renard et al., 2006). The AGP fraction was isolated by gel filtration chromatography and subjected to deglycosylation with hydrofluoric acid (HF) to separate the protein (Qi et al., 1991). About 400 amino acids were contained by the AGP protein fraction ( 33% are... [Pg.6]

Models of regular geometrical pores with rectangular, spherical, cylindrical, and conical shapes have been developed for electrophoresis and gel chromatography media. Figure 7, from Ref 314, gives samples of these uniform structures. These uniform-pore models have been used more extensively in the analysis of gel filtration chromatography. [Pg.544]

Gel filtration chromatography has been extensively used to determine pore-size distributions of polymeric gels (in particle form). These models generally do not consider details of the shape of the pores, but rather they may consider a distribution of effective average pore sizes. Rodbard [326,327] reviews the various models for pore-size distributions. These include the uniform-pore models of Porath, Squire, and Ostrowski discussed earlier, the Gaussian pore distribution and its approximation developed by Ackers and Henn [3,155,156], the log-normal distribution, and the logistic distribution. [Pg.549]

Extraction of Sodium Channel Blockers. A review of published reports shows that methods for purification of sodium channel blockers from bacterial cultures are similar to techniques for isolation of TTX and STX from pufferfish and dinoflagellates (30, 31, 38, 39). Typically, cell pellets of bacterial cultures are extracted with hot 0.1% acetic acid, the resulting supernatant ultra-filtered, lyo-philized, and reconstituted in a minimal volume of 0.1% acetic acid. Culture media can also be extracted for TTX by a similar procedure (Ji). Both cell and supernatant extracts are analyzed further by gel filtration chromatography and other biological, chemical, and immunological methods. Few reports describe purification schemes that include extraction of control samples of bacteriological media (e.g., broths and agars) which may be derived from marine plant and animal tissues. [Pg.79]

Fig. 12 shows a portion of the aliphatic region (30-50 p.p.m.) of the proton-decoupled, C-n.m.r. spectra of fully reductively [ C]methylated glycophorin A" " and glycophorin B. Glycophorin B was isolated from heterozygous, red-blood cells, and was then separated from glycophorin A by gel-filtration chromatography on Ammonyx-Lo. Clearly, the... [Pg.195]

To obtain small xylogalacturonan fragments for further characterization, the EPG digest of the total alkali extract was first separated by gel filtration chromatography on HW-55 S to remove the rhamnogalacturonan (Figure 3). [Pg.84]

It was proved to be a single peak of protein and activity on gel filtration chromatography (figure 4) and single band on SDS-PAGE (figure 5). [Pg.719]

The molecular weight determined by the gel filtration chromatography with Toyopearl 55 HW was 115 kdal while that estimated by SDS-PAGE was 43 kdal (Figure 4,5). [Pg.720]


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Exclusion chromatography gel filtration

Further purification of the microbubble surfactant mixture by gel-filtration column chromatography

Gel filtration

Gel-chromatography

Gel-filtration column chromatography

Gel-filtration column chromatography, amino acid analysis and carbohydrate determination

Gel-filtration/permeation chromatography

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