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  • 1
    Electronic Resource
    Electronic Resource
    Capillary affinophoresis as a versatile tool for the study of biomolecular interactions: a mini-review (1998)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 11 (1998), S. 134-140 
    Details
    ISSN: 0952-3499
    Keywords: affinophoresis ; affinophore ; affinity probe capillary electrophoresis ; pea lectin ; concanavalin A ; laser-induced fluorescence detection ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Combination of capillary electrophoresis and bioaffinity interaction gave rise to powerful research tools for analyzing molecular recognition. They take advantages of the electrophoretic behavior of the complex formed between a target biomolecule and a specially designed mobile ligand molecule (affinophore or affinity probe), and enable detection of complex formation, determination of the equilibrium constants and stoichiometry, etc. Copyright © 1998 John Wiley & Sons, Ltd.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 2
    Electronic Resource
    Electronic Resource
    Specific isolation by anhydrotrypsin-agarose chromatography of a recombinant protein tagged with an affinity tail arginine at the C-terminus (1990)
    Chicester [u.a.] : Wiley-Blackwell
    Journal of Molecular Recognition 3 (1990), S. 204-207 
    Details
    ISSN: 0952-3499
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: A characteristic property of anhydrotrypsin, i.e., its ability to strongly bind C-terminal arginine, proved to be useful as a tool for specific enrichment of a recombinant protein. An arginine tail was introduced at the C-terminus, for example, of a human β-galactoside-binding lectin by site-directed mutagenesis. The resulting mutant recombinant lectin, which retained sugar-binding activity as high as the wild-type lectin, became recognizable by anhydrotrypsin. It was adsorbed on an anhydrotrypsin-agarose column and eluted with benzoylglycylarginine. The added arginine tail could be specifically removed by carboxypeptidase B. When E. coli lyzate containing the mutant lectin was applied to the column more than 10-fold enrichment of the mutant lectin was attained. This procedure should be generally applicable and may be advantageous because the addition of a single arginine residue may have minimal effect on the structure and function of the target protein.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmr.300030506
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  • 3
    Electronic Resource
    Electronic Resource
    Affinophoresis of anti-hapten antibody in rabbit serum with an anionic affinophore bearing the hapten (1987)
    Weinheim : Wiley-Blackwell
    Electrophoresis 8 (1987), S. 135-139 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Affinophoresis is an electrophoretic separation technique for biomolecules using an affinophore, which is a macromolecular polyelectrolyte bearing affinity ligands. It migrates rapidly in an electric field, and consequently the electrophoretic mobility of molecules having affinity for the ligand is specifically changed. An anionic affinophore bearing an antihypertensivepeptide, N-(dibenzyloxyphosphinoyl)-L-alanyl-L-prolyl-L-proline, was synthesized by coupling the peptide to about one-sixth of the amino groups of poly-L-lysine with an average degree of polymerization of 190. The remaining amino groups were succinylated and aminomethanesulfonic acid was coupled to about one-fourth of the succinyl groups by the formation of amide bonds. Electrophoresis of rabbit antiser a raised against the peptide was carried out in an agarosegel plate containing the affinophore. After electrophoresis, separated proteins were transferred to a nitrocellulose sheet and immunoglobulins were visualized by using horseradish peroxidase-conjugated anti-rabbit immunoglobulin G antibody. Hapten-specific antibodies were separated from non-specific antibodies. Two-dimensional agarose gel electrophoresis, in which affinophoresis was used in the second dimension, separated the hapten-specific antibodies from other serum proteins.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150080303
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  • 4
    Electronic Resource
    Electronic Resource
    Affinophoresis of red blood cells: Surface antigen-specific acceleration of electrophoresis (1989)
    Weinheim : Wiley-Blackwell
    Electrophoresis 10 (1989), S. 864-869 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A method employing the technique of affinophoresis to increase the electrophoretic mobility of specific cells according to their surface antigens was developed. Red blood cells were treated consecutively with the maximum subagglutinating dose of an antired blood cell serum, a biotinylated second antibody, avidin and finally with a negatively charged biotin-affinophore which was prepared by coupling biotin to polylysine (average degree of polymerization, 270 or 1150), followed by complete succinylation. The electrophoretic mobility of cells was analyzed with an automatic cell electrophoresis analyzer. The use of a homologous anti-serum increased the electrophoretic mobility of rabbit, human and rat red blood cells by 2.9, 1.7 and 1.6 times, respectively. A larger affinophore containing fewer biotin moieties was more effective. In the case of a mixture of red blood cells from two species, cells from only one species could be accelerated by using homologous antiserum, e.g., affinophoresis of a mixture of human and rat red blood cells by using either homologous antiserum gave two separate peaks on the histogram, whereas a single peak would be obtained in usual electrophoresis because there is little difference in the original migration velocities of the two cell types.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150101212
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  • 5
    Electronic Resource
    Electronic Resource
    Fluorescence-labeled peptides as isoelectric point (pI) markers in capillary isoelectric focusing with fluorescence detection (1995)
    Weinheim : Wiley-Blackwell
    Electrophoresis 16 (1995), S. 1479-1484 
    Details
    ISSN: 0173-0835
    Keywords: Fluorescent pI marker ; Isoelectric focusing ; Capillary electrophoresis ; Laser-induced fluorescence ; Fluorescence-labeled peptides ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Commercially available peptides, mostly angiotensin derivatives, were labeled at their N-terminal amino group with 5-carboxytetramethylrhodamine succinimidyl ester, to obtain fluorescent pI markers for capillary isoelectric focusing with fluorescence detection. The labeled peptides were purified by reversedphase chromatography. They were well separated on isoelectric focusing in a polyacrylamide gel slab and their pIs were determined by comigration with protein-pI markers. The fluorescent markers could be detected as sharp peaks in capillary isoelectric focusing with laser-induced fluorescence detection (He-Ne laser, 1 mW, 543.5 nm). The detection limit was found to be around 3 × 10-12 M (0.8 amol). Tetramethylrhodamine-labeled pea lectin (3 pg) was subjected to capillary isoelectric focusing and the pIs of the fluorescent derivatives of the lectin were determined by using the fluorescence-labeled peptides as pI markers.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501601245
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  • 6
    Electronic Resource
    Electronic Resource
    Capillary affinophoresis of pea lectin with polyliganded affinophores: A model study of divalent-polyvalent interactions (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 397-402 
    Details
    ISSN: 0173-0835
    Keywords: Affinity electrophoresis ; Multivalency ; Affinity constant ; Capillary electrophoresis ; Lectin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Affinophoresis is a type of affinity electrophoresis using an affinophore, a soluble ionic carrier bearing affinity ligand(s). It was reported previously that an affinophore, prepared by coupling multiple p-aminophenyl α-D-mannoside ligands to a part of the carboxyl groups of succinylated polylysine, specifically changed the mobility of pea lectin in agarose gel. The affinophoresis of this divalent lectin with the polyliganded affinophore was investigated by using capillary electrophoresis. Analysis of the mobility change of the lectin in the presence of differently modified affinophores showed that the affinity was larger for affinophores having higher ligand density. Analysis of the inhibition of the mobility change by a neutral ligand, with a known affinity constant for the lectin, allowed estimation of the contributions of monovalent and divalent interactions to the binding in the lectin-affinophore complex. The proportion of divalent complexes was greater for affinophores having higher ligand density. This approach to estimate the contribution of divalency in complex formation should be generally applicable to the analysis of divalent interactions with different techniques other than electrophoresis.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150190306
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  • 7
    Electronic Resource
    Electronic Resource
    Assay of trypsin activity by capillary isoelectric focusing with laser-induced fluorescence detection (1998)
    Weinheim : Wiley-Blackwell
    Electrophoresis 19 (1998), S. 2296-2300 
    Details
    ISSN: 0173-0835
    Keywords: Capillary electrophoresis ; Isoelectric focusing ; Laser-induced fluorescence ; Protease ; Enzyme assay ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Capillary isoelectric focusing is a highly effective method for the separation of proteins due to focusing as a function of their pI values in the separation process. This technique is also effective for certain types of peptides that focus well. Fluorescence labeling and subsequent detection by laser-induced fluorescence farther enhance the sensitivity of this technique. This paper demonstrates the utility of this technique in an enzyme assay. A synthetic nona peptide, H-Gly-Cys-His-Glu-Ala-Arg-Ala-Glu-Glu-OH, was labeled with an iodoacetyl derivative of Lissamine rhodamine B at the thiol group of the cysteine residue as a substrate for trypsin. Trypsin catalyzed the cleavage of the Arg-Ala bond of the labeled substrate, which focused at pH 4.8, and liberated a shortened, labeled product, H-Gly-*Cys-His-Glu-Ala-Arg-OH that focused at pH 6.9 (*indicates the label). The product peptide at 3-300 pM was determined with a relative standard deviation of 5.5% (n = 5) by fluorescence detection at 590 nm with excitation by a green line of He-Ne laser. Incubation of trypsin with the substrate for 10 min at 37°C allowed the determination of 50-250 pg of trypsin, with a relative standard deviation of 5.3% (n = 5).
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150191308
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  • 8
    Electronic Resource
    Electronic Resource
    Influence of a soluble anionic polymer on the electrophoresis of proteins (1989)
    Weinheim : Wiley-Blackwell
    Electrophoresis 10 (1989), S. 238-242 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: The influence of a soluble anionic polymer on electrophoresis of proteins was studied in relation to the nonspecific ionic effect of an affinophore on application to affinophoresis. Zone electrophoresis of proteins was carried out in agarose gel in the presence of succinyl-poly-L-lysine (degree of polymerization, 120) by using three electrophoresis buffers differing in ionic strength (0.06, 0.12 and 0.18) and pH (7.0 and 7.9). Proteins migrated as distinct single bands even in the presence of the polymer. The mobility of cationic proteins towards the cathode was first decreased and then increased towards the anode as the polymer concentration increased, while that of anionic proteins was not affected. The dependence of the apparent mobility changes of the proteins on the concentration of the polymer was treated quantitatively in the same way as affinity electrophoresis. The extent of the ionic interaction between a cationic protein and the polymer could be estimated as an apparent dissociation constant. It greatly depended on the ionic strength of the electrophoresis buffer. Except for the extremely cationic proteins such as lysozyme, the ionic interaction with up to 0.1 mM of the polymer could be practically suppressed by the use of 0.1 M sodium phosphate buffer (pH 7.0).
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150100404
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