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Production system establishment and in vitro study of CD19/CD3ε bite antibody secreted from Pichia pastoris. [PDF]
Sci RepKim B +4 more
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Subunit-specific isotope labelling of heteromeric complexes using cell-free protein expression: application to the 760 kDa ClpXP molecular machine. [PDF]
RSC Chem BiolAudibert A +11 more
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The First Simplified Heparan Sulphate-Alginate Hybrid Trisaccharides: Synthesis and Biological Effects on Human Dermal Fibroblasts. [PDF]
Int J Mol SciKútvölgyi K +9 more
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A Concise Total Synthesis of Tryprostatins A and B and Epimers. [PDF]
ACS OmegaSeideman S +3 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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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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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
openaire +3 more sources