Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Chromatography biospecific

Hoffmann-Ostenhof, O., Breitenbach, M., Roller, F., Kroft, D. and Scheiner, O. (eds.) (1978) Affinity Chromatography, Biospecific Sorption — The First Extensive Compendium on Affinity Chromatography as Applied to Biochemistry and Immunochemistry, Proc. 1st Int. Symp., Vienna, 1977, Pergamon Press, Oxford. [Pg.356]

Egly, J.M. and Porath, J. (1975) in Affinity Chromatography, Biospecific Sorption (Hoffman-Osten-hof, O., et al., eds.) pp. 5-22, Pergamon Press, Oxford. [Pg.357]

Affinity chromatography Biospecific adsorption/desorption Molecular structure... [Pg.303]

Protamine kinase (from rainbow trout testes) [37278-10-7] [EC 2.7.1.70]. Partial purification by hydoxylapatite chromatography followed by biospecific chromatography on nucleotide coupled Sepharose 4B (the nucleotide was 8-(6-aminohexyl)amine coupled cyclic-AMP). [Jergil et al. Biochem J139 441 1974.]... [Pg.562]

Biospecific Chromatography Advantages of Polymer-Spacered Ligands 169... [Pg.135]

Sundberg, L., and Porath, J. (1974) Preparation of adsorbents for biospecific affinity chromatography. [Pg.1119]

Figure 6.14 Schematic representation of the principle of biospecific affinity chromatography. The chosen affinity ligand is chemically attached to the support matrix (agarose bead) via a suitable spacer arm. Only those ligands in solution that exhibit biospecific affinity for the immobilized species will be retained... Figure 6.14 Schematic representation of the principle of biospecific affinity chromatography. The chosen affinity ligand is chemically attached to the support matrix (agarose bead) via a suitable spacer arm. Only those ligands in solution that exhibit biospecific affinity for the immobilized species will be retained...
It is not normally prudent to employ biospecific affinity chromatography as an initial purification step, as various enzymatic activities present in the crude fractions may modify or degrade the expensive affinity gels. However, it should be utilized as early as possible in the purification procedure in order to accrue the full benefit afforded by its high specificity. [Pg.150]

Protein A is a cell-wall protein of Staphylococcus aureus with a molecular weight of 42,000. Since protein A binds specifically to the Fc part of IgG from various animals, it has been widely used in immunoassay and affinity chromatography. We found that protein A could be spread over the water surface to form a monolayer membrane by the LB method [21]. On the basis of this finding, an antibody array on the solid surface can be obtained by the following two steps. The first step is fabrication of an ordered protein A array on the solid surface by the LB method. The second step is self assembly of antibody molecules on the protein A array by biospecific affinity between protein A and the Fc of IgG as shown in Fig.34. [Pg.362]

Biospecific adsorption, 6 396-397, 399 Biospecific binding, in microarray fabrication, 16 385 Biospecific elution, in affinity chromatography, 6 398 Biosphere, selenium occurrence in, 22 78. [Pg.104]

J.A. Lopez-Mas, S.A. Streitenberger, F. Garcia-Carmona and A. Sanchez-Ferrer, Cyclodextrin biospecific-like displacement in dye-affinity chromatography. J.Chromatogr.A, 911(2001) 47-53. [Pg.561]

Similar results were obtained with crude cellulase preparations from Penicillium pinophilum (12). The general applicability of this biospecific chromatography is illustrated by the isolation of the EGD from C. t., cloned in E. c. (Fig. 6). [Pg.576]

A Lundqvist, E Brekkan, L Haneskog, Q Yang, J Miyake, P Lundahl. Determination of transmembrane protein affinities for solutes by frontal chromatography. In P Lundahl, A Lundqvist, E Greijer, eds. Quantitative Analysis of Biospecific Interactions. Amsterdam Harwood Academic, 1998, pp 79-93. [Pg.181]

Table 3.19. Some forms of affinity chromatography that may be employed to purify a selected protein. Virtually all proteins carry out their biological effects by interacting in some way with other molecules, which can be given the general title ligands . This interaction is often quite biospecific. Immobilization of such ligands (or molecules which mimic ligands) onto chromatographic beads thus facilitates selective purification of the molecule of interest... Table 3.19. Some forms of affinity chromatography that may be employed to purify a selected protein. Virtually all proteins carry out their biological effects by interacting in some way with other molecules, which can be given the general title ligands . This interaction is often quite biospecific. Immobilization of such ligands (or molecules which mimic ligands) onto chromatographic beads thus facilitates selective purification of the molecule of interest...
Ion exchange chromatography, hydrophobic interaction chromatography (HlC), and affinity chromatography (AC) show some similarities concerning practical realization therefore, most of the hints given for lEC are applicable for HlC and AC. Examples for AC are given in Protocols 3.6.2.4 (biospecific desorption) and 3.6.2.5 (elution by partial denaturation). [Pg.102]


See other pages where Chromatography biospecific is mentioned: [Pg.44]    [Pg.745]    [Pg.314]    [Pg.5]    [Pg.513]    [Pg.745]    [Pg.44]    [Pg.745]    [Pg.314]    [Pg.5]    [Pg.513]    [Pg.745]    [Pg.57]    [Pg.2063]    [Pg.126]    [Pg.169]    [Pg.170]    [Pg.394]    [Pg.285]    [Pg.80]    [Pg.81]    [Pg.169]    [Pg.9]    [Pg.140]    [Pg.149]    [Pg.150]    [Pg.142]    [Pg.167]    [Pg.166]    [Pg.371]    [Pg.371]    [Pg.372]    [Pg.623]    [Pg.140]    [Pg.89]    [Pg.163]    [Pg.408]   
See also in sourсe #XX -- [ Pg.25 ]

See also in sourсe #XX -- [ Pg.26 ]

See also in sourсe #XX -- [ Pg.28 ]

See also in sourсe #XX -- [ Pg.28 ]




SEARCH



© 2024 chempedia.info