Results 241 to 250 of about 735,127 (280)
Rapid purification of brain protein complexes containing active and inactive forms of the G protein Gαo. [PDF]
PLoS OneYadav S +4 more
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Gnetumgams A and B: two new 2-phenylbenzofuran derivatives from the lianas of <i>Gnetum montanum</i> with xanthine oxidase inhibitory activity. [PDF]
RSC AdvVan Do TN +4 more
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Reproducibility of gel‐chromatography
International Journal of Peptide and Protein Research, 1984We think it worthwhile to other experimenters to mention the following observations. Recently it was noted that gel chromatographic separations of the five fragments resulting from the degradation of cytochrome c by bromocyanogen became dependent on the batch number of the gel. This dependency concerns only separations of unprotected fragments, using 7%
Tesser, G.I. +3 more
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Journal of Chromatography B: Biomedical Sciences and Applications, 1981
It is assumed that heparin is a heterogeneous substance. In order to further investigate the purification of heparin, a column chromatographic technique for the fractionation of heparin is described using various diameters of bead form cross-linked dextran gels and an automated apparatus. It was observed that Sephadex G-50 resulted in the separation of
R, Losito, H, Gattiker, G, Bilodeau
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It is assumed that heparin is a heterogeneous substance. In order to further investigate the purification of heparin, a column chromatographic technique for the fractionation of heparin is described using various diameters of bead form cross-linked dextran gels and an automated apparatus. It was observed that Sephadex G-50 resulted in the separation of
R, Losito, H, Gattiker, G, Bilodeau
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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 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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Angewandte Chemie International Edition in English, 1970
AbstractGel chromatography can be regarded as a network‐limited partitioning of substances. The theory of this method and the preparation and properties of various gel systems are reviewed. Optimization of the method is illustrated for the separation of oligomers.
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AbstractGel chromatography can be regarded as a network‐limited partitioning of substances. The theory of this method and the preparation and properties of various gel systems are reviewed. Optimization of the method is illustrated for the separation of oligomers.
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