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Biomolecules affinity partitioning

Other applications besides purification of biomolecules are affinity partitioning (Labrou, 1994), extractive bioconversions (Andersson, 1990 Kaul, 1991 Zijlstra, 1998), liquid-liquid partition chromatography, and analytical assays. Although industrial applications of aqueous two-phase systems have not gained widespread use to date, practical and economic feasibility has been proved (Tjemeld, 1990 Cunha, 2002). [Pg.231]

TABLE 11 Affinity Partitioning of Biomolecules in Aqueous Two-Phase Systems... [Pg.356]

Some recent developments in this area, which resulted in either increase in selectivity or improvement in yield, are briefly discussed here. Affinity partitioning (AP) is based on the preferential/biospecific interaction between the molecule and affinity polymer derivative which results in a biomolecule-polymer derivative complex which selectively partitions to one of the phases leaving the contaminating substances or proteins in the other phase. Most of the reported investigations regarding affinity partitioning pertain to polymer/... [Pg.171]

For more polar components, the bonded normal phase supports are particularly useful and have benefits over adsorption chromatography on silica by allowing a rapid response to solvent composition changes. Other modes of partition chromatography, such as Ugand-exchange and affinity chromatography, have found particular applications for the resolution of water-soluble biomolecules. [Pg.118]

In 1993, Hutchens and co-workers described surface-enhanced laser desorption/ionization (SELDI) technique, an affinity technology, which has progressed over the last decade to become a powerful analytical, an on-plate approach (Hutchens and Yip 1993). SELDI is a distinctive form of laser desorption/ionization (LDI) mass spectrometry in which the EDI probe plays an active role in the homogenization, preconcentration, amplification, purification, extraction, enrichment digestion, derivatization, synthesis, separation, and detection with complementary techniques, prior to the desorption and ionization of the analytes by MALDI (Merchant and Weinberger 2000). The principle of this approach is very simple. Biomolecules are captured by adsorption, partition, electrostatic interaction, or affinity chromatography on a solid-phase protein chip surface. Although SELDI provides a unique sample preparation platform, it is similar to MALDI-MS in that a laser... [Pg.772]


See other pages where Biomolecules affinity partitioning is mentioned: [Pg.77]    [Pg.357]    [Pg.2232]    [Pg.25]    [Pg.2216]    [Pg.717]    [Pg.238]    [Pg.227]    [Pg.10]    [Pg.357]    [Pg.89]    [Pg.227]    [Pg.1280]    [Pg.227]    [Pg.474]    [Pg.119]    [Pg.1945]    [Pg.128]    [Pg.1208]    [Pg.240]    [Pg.91]   
See also in sourсe #XX -- [ Pg.356 , Pg.357 ]




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