(1987) A simple histochemical method for locating enzymes in plant tissue using nitrocellulose blotting. (1992) A simple method to increase resolution in whole leaf blotting. (1984) A quantitative dot-immunobinding assay for proteins using nitrocellulose membrane filters. Jahn, R., Schiebler, W., and Greengard, P.(1987) Comparative sensitivity of 125I-Protein A and enzyme-conjugated antibodies for detection of immunoblotted proteins. (1990) Double staining of immunoblot using enzyme histochemistry and india ink. (1984) A rapid, sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on Western blots. (1986) Reversible staining and peptide mapping of proteins transferred to nitrocellulose after separation by sodium dodecylsulphate-polyacrylamide gel electrophoresis. (1986) The effect of staining on the immunoreactivity of nitrocellulose-bound proteins. (1985) Sensitive colloidal metal (gold and silver) staining of protein blots on nitrocellulose membranes. Moeremans, M., Daneels, G., and De Mey, J.(1983) India ink staining of proteins on nitrocellulose paper. (1987) Characterisation of monoclonal antibodies to protoplast membranes of Nicotiana tabacum identified by an enzyme-lurked immunosorbent assay. (1986) Immunoblotting with monoclonal antibodies: Importance of the blocking solution. H., and Thorpe, R (1988) The use of Tween 20 alone as a blocking agent for immunoblotting can cause artefactual results. (1986) Rapid and effective transfer of integral membrane proteins from isoelectric focusing gels to nitrocellulose membranes. (1982) Vacuum-blotting: a new simple and efficient transfer of proteins from sodium dodecylsulphate-polyacrylamide gels to nitrocellulose. Peferoen, M., Huybrechts, R., and De Loof, A.(1991) Blotting of seed proteins from isoelectrically focused gels for cultivar identification. (1982) Protein transfer from isoelectric focusing gels: The native blot. (1980) The detection of DNA-binding proteins by protein blotting. (1991) Evaluation of membranes used for electroblotting of proteins for direct automated microsequencing. (1981) “Western Blotting” Electrophoretic transfer of proteins from sodium dodecylsulphate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated Protein A. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose Procedure and some applications. Towbin, H., Staehelin, T., and Gordon, J.(1975) Detection of specific sequences among DNA fragments separated by gel electrophoresis. (1991) The expression of a chimeric cauliflower mosaic virus (CaMV-35S)-pea vicilin gene in tobacco. These are analysis of tissue extracts using dot blotting, and “squash” blots of whole plants or plant organs. In addition, we will discuss two other applications of protein blotting that provide rapid but less precise results. We will initially discuss these options, and then provide detailed step-by-step instructions for a well-established method of protein transfer and identification using an enzyme-labeled second antibody. This is commonly called Western blotting, and provides the operator with a wide range of options for choice of membrane type, transfer system, and detection system. The approach is usually applied to protein transferred from electrophoretic separations ( seeChapter 34 ), which allows positive identification to be combined with the provision of information about the protein M r charge, pI, and so on. The immunodetection of proteins bound to a membrane has widespread applications in plant biochemistry and molecular biology, including the identification and semiquantitative determination of foreign proteins expressed in transgenic plants.
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