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  • 1985-1989  (5)
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Material
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Year
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  • 1
    Electronic Resource
    Electronic Resource
    Effect of histidine residues in antigenic sites on pH dependence of immuno-adsorption equilibrium (1988)
    Springer
    Applied microbiology and biotechnology 27 (1988), S. 528-532 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Polyclonal anti-myoglobin antibodies were fractionated into five subpopulations directed against five specific antigenic sites, respectively. The equilibrium characteristics of each subpopulation and orginal anti-myoglobin immobilized to CNBr-activated Sepharose 4B were compared. The four subpopulations of antibodies lost their binding abilities at around pH 4.5 because of the conformational changes of myoglobin. However, the subpopulation directed against the region containing three histidine residues dissociated with the antigenic site at higher pH, and such equilibrium characteristics were considered to be caused by the dissociation characteristics of histidine residues. Therefore, the effects of histidine modification in BSA on the adsorption capacities of original anti-BSA antibody and a pH sensitive fraction of it were compared. The adsorption capacity of the pH sensitive fraction showed greater decrease than that of original antibody by histidine modification in BSA. These results imply that the antigenic sites in which histidine residues play an important role for the binding to antibodies show equilibrium characteristics sensitive to pH.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00451626
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Effects of charged groups in haptens on adsorption equilibrium of hapten antibody (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 32 (1988), S. 467-474 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Antisera against charged (p-azobenzoate and p-azoben zenesulfonate) and uncharged (dinitrophenyl) haptenic groups were produced in rabbits, and the equilibrium characteristics of hapten-antibody were measured by use of immunoadsorbents. The antibody to the uncharged hapten formed a stable binding with the hapten to the changes in ionic strength and pH. On the other hand, the antibodies to the charged haptens showed affinities sensitive to the changes in pH and ionic strength. Therefore, the effect of the pKa of ionizable haptens on the pH dependence of the hapten-antibody binding was studied by comparing the interactions between a series of para-substituted benzoic acids and the anti-p-azobenzoate antibody. The pH dependence of the interactions was strongly affected by the pKa of ionizable groups in haptens. Furthermore, the equilibrium characteristics of anti-p-aminobenzoyl dipeptides were compared. The characteristics of interactions were affected by the features of amino acid residues.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260320409
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Adsorption equilibrium in immuno-affinity chromatography with polyclonal and monoclonal antibodies (1986)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 28 (1986), S. 1497-1502 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The effects of pH, ionic strength, anion species, and antibody concentration on the adsorption equilibrium between immobilized antibodies and antigens were studied by use of anti-BSA, anti-HSA, anti-BlgG, and monoclonal anti-HSA coupled to Sepharose 4B. The polyclonal antibodies possessed average binding affinities of the order of 108M-1, and the heterogeneity was accounted for by assuming a normal distribution of the free energy of antibody-antigen combination. The monoclonal antibody, on the other hand, showed a homogeneous affinity of the Langmuir type. Bound antigens could be eluted by lowering pH or adding a chaotropic anion, and their purity was very high. The antibody ligand was sufficiently stable for repeated use.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260281007
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Characterization of fractionated polyclonal antibodies for immunoaffinity chromatography (1988)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 31 (1988), S. 635-642 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Polyclonal anti-BSA antibodies were ractionated by stepwise elution from an immobilized BSA column by decreasing pH or increasing the concentration of NaSCN. The binding affinities of each fraction and original globulin under physiological conditions and their dependence on pH and ionic environments were compared. Fractions with high association constant under physiological conditions did not necessarily show antigen binding affinity over a wide pH range, but they retained a high affinity at higher ionic strength of NaSCN. Consequently, by combining these two fractionation procedures, a fraction with high affinity and which dissociated at moderate pH was obtained. It is clear that high affinity is not always incompatible with ease of dissociation accompanying a change in conditions.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260310702
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Improvement of proteolytic resistance of immunoadsorbents by chemical modification with polyethylene glycol (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 34 (1989), S. 532-540 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Immunoadsorbents were modified with monomethoxy-polyethylene glycol (PEG; average molecular weights of 5000 (PEG-5000) and 1900 (PEG-1900)) activated with cyanuric acid (activated PEG) by four different methods. In the two methods, anti-BSA antibodies were modified with activated PEG with and without protection of antigen binding sites with BSA and then were coupled to CNBr-activated Sepharose 4B. In the other two methods, Immunoadsorbents, which were prepared by coupling anti-BSA antibodies to CNBr-activated Sepharose 4B, were modified with activated PEG with and without the protection. The effects of PEG modification by these four methods on the binding ratio (the ratio of the numbers of moles of antigen adsorbed to the numbers of moles of binding sites of antibody coupled), the antigen binding property and the resistance to proteolytic digestion of immunoadsorbents were studied. The decrease in the binding ratio by the modification with activated PEG was small enough to use modified immunoadsorbents for industrial purification processes. The resistance to proteolytic digestion of immunoadsorbents was improved by modification with activated PEG. The modification without protection of antigen binding sites gave higher resistance to proteolytic digestion than that with protection, while the former caused larger decrease in the binding ratio of modification. The immunoadsorbents modified with activated PEG-5000 showed higher resistance to proteolytic digestion than those modified with activated PEG-1900.
    Additional Material: 14 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260340413
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    Paper (German National Licenses)
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