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Current Protocols in Molecular Biology, 1998
AbstractGel filtration (GF) chromatography separates proteins solely on the basis of molecular size. Separation is achieved using a porous matrix to which the molecules, for steric reasons, have different degrees of access‐‐i.e., smaller molecules have greater access and larger molecules are excluded from the matrix. Hence, proteins are eluted from the
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AbstractGel filtration (GF) chromatography separates proteins solely on the basis of molecular size. Separation is achieved using a porous matrix to which the molecules, for steric reasons, have different degrees of access‐‐i.e., smaller molecules have greater access and larger molecules are excluded from the matrix. Hence, proteins are eluted from the
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Gel diffusion chromatography of dextran
Journal of Chromatography A, 1962Abstract Glucose and dextrans of molecular weight 5,000 to 300,000 can be partially separated chromatographically on columns of agar (6–9 %) with buffer (pH 8.0) or water as eluant. Agarose gels (4 %) can also be used with water as eluant. The method can be used to estimate approximately the molecular weight distribution in small samples of clinical ...
B C, HUMMEL, D C, SMITH
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Gel matrices for scanning gel chromatography
Biophysical Chemistry, 1979I have examined the light-scattering behavior of a number of gel matrices used in gel filtration chromatography. The angular dependence of light scattering by Sephadexes is consistent with treatment of the particles as large scattering particles with a low refractive index increment (mu).
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Gel Permeation Chromatography of Heparins
Thrombosis and Haemostasis, 1980SummaryGel 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.
B, Mulloy, E A, Johnson
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Bacteriophage purification by gel chromatography
Analytical Biochemistry, 1981Abstract We have developed an inexpensive procedure for bacteriophage purification suitable for small- and medium-scale preparations (up to one liter of lysate). The method consists of precipitation with polyethylene glycol 6000 and gel chromatography on a Bio-Gel A-5m column. The purity of the phage preparation is comparable to that obtained by CsCl
B, Sain, S, Erdei
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Fluorinated gels for gel permeation chromatography
Die Makromolekulare Chemie, 1993AbstractThe aim of these investigations was the development of stationary phases for GPC compatible with fluorinated solvents. The properties of crosslinked copolymers of 4‐(2‐heptafluoropropoxy‐1, 2,2‐trifluoroethoxy)styrene (1) were investigated in dependence of the mode of synthesis. Divinylbenzene (DVB) was used as crosslinking agent.
Hans‐Jürgen Juhl, Walter Heitz
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Gel chromatography of carbohydrates on polysaccharide gel
Journal of Polymer Science: Polymer Symposia, 1980AbstractLiquid chromatographies of high and low‐molecular carbohydrates and polyethyleneglycols of different molecular masses were studied on porous microspherical cellulose. Dependence of the distribution coefficients of polymer molecules on molecular mass was determined.
Yu. A. Eltekov +4 more
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Determination of the structure of agarose gels by gel chromatography
Biochimica et Biophysica Acta (BBA) - General Subjects, 1967Abstract Well-characterized fractions of the synthetic polysaccharide Ficoll have been chromatographed on columns of pearl-condensed agarose gels of concentrations between 2 and 8%. The results agree with the theory that the Ficoll is sterically excluded from the gel, which is made up of a random three-dimensional network of long fibers.
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The determination of myoglobin by gel chromatography
Analytical Biochemistry, 1978Abstract The method recently described for the determination of haemoglobin in ovine muscles (1) has now been modified for the measurement of myoglobin. Evidence is presented here for the validity of using it for myoglobin determination in muscles of the rat, pig, sheep, and ox.
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Chromatography of glycogens on agarose gels
Journal of Chromatography A, 1973Abstract The chromatographic behavior of several glycogens on the agarose gels Sepharose 2B and Sepharose 4B has been investigated. These are shown to be convenient media for examination of the polydispersity and relative molecular weights of different glycogens.
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