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  • 1
    Electronic Resource
    Electronic Resource
    Polycomplexes – potential for bioseparation (1998)
    Springer
    Bioseparation 7 (1998), S. 207-220 
    Details
    ISSN: 1573-8272
    Keywords: polyelectrolytes ; polycomplexes ; protein isolation ; protein–polyelectrolyte complexes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract This review discusses the properties of complexes formed by proteins with polyelectrolytes (PPC) and two polyelectrolyte molecules of opposite charge (PEC). The most highly charged polymers with ionic groups in each monomer unit are considered in this paper. There are all reasons to regard PEC as macromolecular compounds produced as a result of equilibrium reactions with inherent permanent exchange of polyions in water-salt solutions. They combine two properties that might appear at first sight to be mutually exclusive, i.e. rather high stability and lability. Introduction of bioaffinity ligands endows PEC with the recognition capacity sufficient for the purposes of bioseparation and bioanalysis. Antibody-PEC conjugates were successfully used in the immunoassay combining the advantages of both homogeneous and heterogeneous assays and for modeling of chaperone action. The unique properties of polyelectrolyte complexes in combination with bioaffinity ligands makes them promising for the development of highly efficient means of protein isolation, new immunoassay procedures and creation of reversibly soluble biocatalysts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008007818765
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Affinity chromatography of neoglycoproteins (2000)
    Springer
    Bioseparation 9 (2000), S. 315-323 
    Details
    ISSN: 1573-8272
    Keywords: affinity chromatography ; boronate chromatography ; concanavalin A chromatography ; neoglycoprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Glycoproteins, as a class of biomolecules, exhibit much more heterogeneous structures than non-glycosylated proteins. They present a challenging area of research. Model glycoproteins with well-defined protein and carbohydrate structures are helpful in the search for high-resolution methods for the separation of glycoproteins. Neoglycoproteins, maltose-modified chymotrypsin and lactose-modified chymotrypsin, were synthesised by modifying chymotrypsin with maltose and lactose, respectively, using the reductive amination method. Boronate chromatography was applied to isolate the neoglycoproteins from non-glycosylated substances. The use of Tris–HCl as a shielding reagent during the boronate chromatography proved to be efficient in eliminating unwanted interactions between the boronate ligand and the peptide backbone of chymotrypsin. The retention time of neoglycoproteins on the boronate column was increased with increasing the degree of modification.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1011187724356
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Shielding Affinity Chromatography (1994)
    [s.l.] : Nature Publishing Company
    Nature biotechnology 12 (1994), S. 1086-1086 
    Details
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] Pulsing your columns with polymers prevents nonspecific binding and allows elution by temperature ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nbt1194-1086
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Aqueous two-phase system formed by thermoreactive vinyl imidazole/vinyl caprolactam copolymer and dextran for partitioning of a protein with a polyhistidine tail (1997)
    Springer
    Biotechnology techniques 11 (1997), S. 231-236 
    Details
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A new type of aqueous two-phase system (ATPS) has been developed for application combining two attractive concepts in downstream processing: the immobilised metal affinity partitioning and the use of thermoprecipitating polymers. ATPS consisting of the thermoprecipitating copolymer of N-vinyl caprolactam/1-vinyl imidazole loaded with Cu ions (Cu-poly-VI-VCL) in the top phase and dextran T70 in the bottom phase was used for purification of recombinant lactate dehydrogenase carrying an affinity tag of 6 histidine residues (His-LDH ) from a crude E. coli extract. The enzyme partitioned preferentially into the top Cu-poly-VI-VCL-rich phase. After phase separation, the latter was mixed with EDTA. Temperature increase to 45°C resulted in thermoprecipitation of VCL/VI-polymer, which could subsequently be recycled. His-LDH remained solubilized in the aqueous phase resulting in 8-fold purification and 80 % recovery in a single step.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018430319981
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Affinity thermoprecipitation of trypsin using soybean trypsin inhibitor conjugated with a thermo-reactive polymer, poly(N-vinyl caprolactam) (1992)
    Springer
    Biotechnology techniques 6 (1992), S. 353-358 
    Details
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The soybean trypsin inhibitor conjugate with a thermo-reactive water soluble polymer, poly(N-vinyl caprolactam), was successfully used for thermally induced affinity precipitation of trypsin. The validity of the developed procedure was proven by a model separation of trypsin from dilute solution containing a large excess of bovine serum albumin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02439325
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Dye-affinity techniques for bioprocessing: Recent developments (1996)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 9 (1996), S. 259-274 
    Details
    ISSN: 0952-3499
    Keywords: textile dyes ; triazine dyes ; protein purification ; affinity chromatography ; affinity partitioning ; affinity precipitation ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Textile or triazine dyes play an important role as affinity ligands in protein purification. Each step of the protein purification protocol can be divided into three stages, partitioning between two phases, separation of these phases and recovery of the target protein from the enriched phase. Now developments in dye-affinity techniques are discussed emphasizing the innovations in all three stages of the protein purification process. Dye-affinity chromatography has become a routine step in protein purification. New dyes have been developed and used successfully in both traditional chromatographic mode and new modes like affinity precipitation, polymer aqueous two-phase partitioning or expanded bed chromatography. The specificity of dye techniques has been increased by both purposeful designing of new dyes and decreasing non-specific protein-dye interactions with polymer shielding. One can envisage further development and ramification of dye-affinity techniuqes in protein purification.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 7
    Electronic Resource
    Electronic Resource
    Polymer-shielded dye-affinity chromatography (1996)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 9 (1996), S. 509-514 
    Details
    ISSN: 0952-3499
    Keywords: triazine dyes ; poly(N-vinylpyrrolidone) ; poly(vinyl alcohol) ; dye-affinity chromatography ; protein purification ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Polymer-shielded dye-affinity chromatography is a form of chromatography in which the dye matrix forms complexes with a nonionic, water-soluble polymer such as poly(vinylpyrrolidone) or poly(vinyl alcohol), prior to the column chromatography of a crude protein extract, the idea being that polymer shielding of the dye will prevent nonspecific interactions between the target protein and the dye. The concept of polymer shielding and a strategy for the rational selection of polymers suitable as shielding agents are presented.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 8
    Electronic Resource
    Electronic Resource
    Protein displacement in dye-ligand chromatography using neutral and charged polymers (1998)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 11 (1998), S. 255-260 
    Details
    ISSN: 0952-3499
    Keywords: displacement ; dye-ligand chromatography ; polymer ; poly(ethylene imine) ; poly(N-vinyl pyrrolidone) ; poly(N-vinyl caprolacatam) ; protein purification ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Displacement chromatography was demonstrated to perform separations efficiently under mass-overloaded conditions, offering advantages such as increased product recovery and purity, superior resolving power, and concentration and purification in a single processing step. The use of water-soluble polymers for protein displacement in dye-ligand chromatography was initiated in our laboratory. The polymers for displacement were selected using difference spectroscopy to monitor their interactions with a dye-ligand in solution. Non-charged polymers such as poly(N-vinyl pyrrolidone) and poly(N-vinyl caprolactam) efficiently displaced lactate dehydrogenase from porcine muscle from a Blue Sepahrose column. The latter polymer, being thermosensitive, could be easily removed from the eluate and recovered by precipitation at 45 °C and low-speed centrifugation. The positively charged polymer poly(ethylene imine) proved to be an even more efficient displacer. The dye-ligand column could be regenerated after application of displacer either by washing with a solution of the soluble ligand Cibacron Blue (in the case of non-charged polymers) or by washing with highly alkaline solutions containing polyanions (in the case of poly(ethylene imine)) The latter formed a soluble complex with poly(ethylene imine) and stripped the column from the polymer. Copyright © 1998 John Wiley & Sons, Ltd.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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