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  • 1
    Electronic Resource
    Electronic Resource
    Antibodies bound to nitrocellulose in acidic buffers retain biological activity (1993)
    Weinheim : Wiley-Blackwell
    Electrophoresis 14 (1993), S. 886-891 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: This report compares the binding of proteins to nitrocellulose membranes in acidic buffers (pH 2 and 3) with binding in neutral buffer (pH 7). Initially, similar amounts of antibodies and other proteins bound to the nitrocellulose membrane in both acidic and neutral buffers. However, the susceptibility of individual proteins to displacement (stripping) from the membrane by the milk blocking agent depended on the pH of the buffer used to bind the proteins to the membrane. Most proteins that bound to nitrocellulose in acidic buffers were relatively resistant to milk-stripping compared to proteins bound in pH 7 buffer. Acid-binding of proteins to nitrocellulose also decreased the amount of protein that was stripped from the nitrocellulose membrane when Tween 20 was included in the washing buffer. After correcting for the amount of antibody remaining on the membrane after the milk block, it was found that acid-bound antibodies were unchanged in biological activity when compared with the same antibodies bound at neutral pH. These results suggest that acid-binding of proteins could increase the sensitivity of nitrocellulose membrane assays that use milk and/or Tween 20.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.11501401141
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Rehydratable agarose gels: Application to isoelectric focusing in 9 molar urea (1989)
    Weinheim : Wiley-Blackwell
    Electrophoresis 10 (1989), S. 741-747 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: A method is described for the preparation of rehydratable agarose gels, with specific application to the direct incorporation of 9 M urea and carrier ampholytes into rehydratable agarose gels for use in isoelectric focusing. After drying the agarose gel containing an uncharged linear polyacrylamide, one gel volume of a 9 M urea-carrier ampholyte solution is absorbed directly into the gel in 60 min, eliminating equilibration or dialysis of the gel in larger volumes of the 9 M urea-carrier ampholyte solution. Proteins with a molecular mass of 970 000 Da can be separated by isoelectric focusing in these rehydratable gels. The focused proteins can then be quantitatively transferred to nitrocellulose in less than 10 min, and any immunostaining procedure can be used to probe the blotted proteins. These agarose gels are easy to make, they rehydrate rapidly and they can be used in applications other than isoelectric focusing.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150101102
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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