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  • 1990-1994  (1)
  • 1985-1989  (3)
  • Chemistry  (4)
  • 1
    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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    Paper (German National Licenses)
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  • 2
    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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    Paper (German National Licenses)
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  • 3
    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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    Paper (German National Licenses)
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  • 4
    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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    Paper (German National Licenses)
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