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Detektion von Protein und Nucleinsäure auf Membran

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Gentechnische Methoden
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Zusammenfassung

Beim Protein-Blotting werden Proteine auf eine Membran überführt und dort einer Nachweisreaktion unterzogen, die für ein Protein spezifisch ist oder sein soll. Die Proteine werden dazu entweder direkt auf die Membran getüpfelt (Dot-Blot) oder sie werden gelelektrophoretisch getrennt und anschließend aus dem Gel auf die Membran transferiert (Gel-Blot). Je nach Aufbau des Experiments erhält man dabei entweder Informationen über die tatsächliche Spezifität der Nachweisreaktion oder eine Aussage über Eigenschaften und Menge des Proteins. Das Blotten der Proteine auf eine Membran bietet dabei den Vorteil, dass die Membran als Trägermatrix einfacher zu handhaben ist als ein Gel. Die Proteine auf der Membranoberfläche sind immobilisiert und so auch für voluminöse Nachweisreagenzien gut zugänglich.

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Literatur

  • Abidi, F.E., Roh, H., Keath, E.J. (1998): Identification and Characterization of a Phase-Specific, Nuclear DNA Binding Protein from the Dimorphic Pathogenic Fungus Histoplasma Capsulatum. Infect. Immun. 66, 3867–3873.

    PubMed  CAS  Google Scholar 

  • Akhavan-Tafti, H., DeSilva, R., Arghavani, Z., Eickholt, R., Handley, R.S., Schoenfelner, B.A., Sugioka, K., Sugioka, Y., Schaap, A.P. (1998): Characterization of Acridincarboxylic Acid Derivatives as Chemiluminescent Peroxidase Substrates. J. Org. Chem. 63, 930–937.

    Article  CAS  Google Scholar 

  • Akhavan-Tafti, H., Xie, W., DeSilva, R., Cripps, W.G., Eickholt, R.A., Handley, R.S., Linsky, R.S., Mazelis, M.E., Schaap, A.P. (2004): Robust New Chemiluminescent Peroxidase Substrates. IVD Technology 10(4), 33–39.

    Google Scholar 

  • Aizawa, K., Gantt, E. (1998): Rapid Method for Assay of Quantitative Binding of Soluble Proteins and Photosynthetic Membrane Proteins on Poly(vinylidene difluoride) Membranes. Anal. Chim. Acta 365, 109–113.

    Article  CAS  Google Scholar 

  • Bjerrum, O.J., Selmer, J.C., Lihme, A. (1987): Native Immunoblotting. Transfer of Membrane Proteins in the Presence of Nonionic Detergent. Electrophoresis 8, 388–397.

    Article  CAS  Google Scholar 

  • Blake, M.S., Johnston, K.H., Russell-Jones, G.J., Gotschlich, E.C. (1984): A Rapid, Sensitive Method for Detection of Alkaline Phosphatase-Conjugated Anti-Antibody on Western Blots. Anal. Biochem. 136, 175–179.

    Article  PubMed  CAS  Google Scholar 

  • Bobrow, M.N., Shaughnessy, K.J., Litt, G.J. (1991): Catalyzed Reporter Deposition, a Novel Method of Signal Amplification. II. Application to Membrane Immunoassays. J. Immunol. Methods 137, 103–112.

    Article  PubMed  CAS  Google Scholar 

  • Bolt, M.W., Mahoney, P.A. (1997): High-Efficiency Blotting of Proteins of Diverse Sizes Following Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis. Anal. Biochem. 247, 185–192.

    Article  PubMed  CAS  Google Scholar 

  • Brand, J.A., Tsang, V.C.W., Zhou, W., Shukla, S.B. (1990): Comparison of Particulate 3,3’,5,5’-Tetramethylbenzidine and 3,3’-Diaminobenzidine as Chromogenic Substrates for Immunoblot. BioTechniques 8, 58–60.

    PubMed  CAS  Google Scholar 

  • Bronstein, I., Voyta, J.C., Murphy, O.J., Bresnick, L., Kricka, L.J. (1992): Improved Chemiluminescent Western Blotting Procedure. BioTechniques 12, 748–753.

    PubMed  CAS  Google Scholar 

  • Burnette, W.N. (1981): Western Blotting. Electrophoretic Transfer of Proteins from Sodium Dodecyl Sulfate-Polyacrylamide Gels to Unmodified Nitrocellulose and Radiographic Detection with Antibody and Radioiodinated Protein A. Anal. Biochem. 112, 195–203.

    Article  PubMed  CAS  Google Scholar 

  • Chu, N.M., Jankila, A.J., Wallace, J.H., Yam, L.T. (1989): Assessment of a Method for Immunochemical Detection of Antigen on Nitrocellulose Membranes. J. Histochem. Cytochem. 37, 257–263.

    Article  PubMed  CAS  Google Scholar 

  • De Blas, A.L., Cherwinski, H.M. (1983): Detection of Antigens on Nitrocellulose Paper Immunoblots with Monoclonal Antibodies. Anal. Biochem. 133, 214–219.

    Article  PubMed  Google Scholar 

  • Demeulemester, C., Peltre, G., Laurent, M., Pankeleux, D., David, B. (1987): Cyanogen Bromide-Activated Nitrocellulose Membranes. A New Tool for Immunoprint Techniques. Electrophoresis 8, 71–73.

    Article  CAS  Google Scholar 

  • Egger, D., Bienz, K. (1994): Protein (Western) blotting. Mol. Biotechnol. 1, 289–305.

    Article  PubMed  CAS  Google Scholar 

  • Esen, A., Conroy, J.M., Wang, S.Z. (1983): A Simple and Rapid Dot-Immunobinding Assay for Zein and other Prolamins. Anal. Biochem. 132, 462–467.

    Article  PubMed  CAS  Google Scholar 

  • Fowler, S.J. (1994): The Detection of Proteins on Blots Using Gold or Immunogold. Methods Mol. Biol. 32, 239–255.

    PubMed  CAS  Google Scholar 

  • Goso, Y., Hotta, K. (1994): Dot-Blot Analysis of Rat Gastric Mucin Using Histochemical Staining Methods. Anal. Biochem. 223, 274–279.

    Article  PubMed  CAS  Google Scholar 

  • Greenspan, P., Fowler, S.D. (1985): Spectrofluorometric Studies of the Lipid Probe, Nile Red. J. Lipid Res. 26, 781–789.

    PubMed  CAS  Google Scholar 

  • Gültekin, H., Heermann, K.H. (1988): The Use of Polyvinylidenedifluoride Membranes as a General Blotting Matrix. Anal. Biochem. 172, 320–329.

    Article  PubMed  Google Scholar 

  • Gupta, S.K., Masinick, S., Garrett, M., Hazlett, L.D. (1997): Pseudomonas Aeruginosa Lipopolysaccharide Binds Galectin-3 and Other Human Corneal Epithelial Proteins. Infect. Immun. 65, 2747–2753.

    PubMed  CAS  Google Scholar 

  • Harlow, E., Lane, D. (Hrsgg.) (1988): Antibodies, a Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, pp. 471–510.

    Google Scholar 

  • Haselbeck, A., Schickaneder, E., von der Eltz, H., Hosel, W. (1990): Structural Characterization of Glycoprotein Carbohydrate Chains by Using Digoxigenin-Labeled Lectins on Blots. Anal. Biochem. 191, 25–30.

    Article  PubMed  CAS  Google Scholar 

  • Hawkes, R., Niday, E., Gordon, J. (1982): A Dot-Immunobinding Assay for Monoclonal and Other Antibodies. Anal. Biochem. 119, 142–147.

    Article  PubMed  CAS  Google Scholar 

  • Heinicke, E., Kumar, U., Munoz, D.G. (1992): Quantitative Dot-Blot Assay for Proteins Using Enhanced Chemiluminescence. J. Immunol. Methods 152, 227–236.

    Article  PubMed  CAS  Google Scholar 

  • Heukeshoven, J., Dernick, R. (1995): Effective Blotting of Ultrathin Polyacrylamide Gels Anchored to a Solid Matrix. Electrophoresis 16, 748–756.

    Article  PubMed  CAS  Google Scholar 

  • Hoffman, W.L., Jump, A.A., Kelly, P.J., Ruggles, A.O. (1991): Binding of Antibodies and Other Proteins to Nitrocellulose in Acidic, Basic, and Chaotropic Buffers. Anal. Biochem. 198, 112–118.

    Article  PubMed  CAS  Google Scholar 

  • Hoffman, W.L., Jump, A.A., Ruggles, A.O. (1994): Soaking Nitrocellulose Blots in Acidic Buffers Improves the Detection of Bound Antibodies without Loss of Biological Activity. Anal. Biochem. 217, 153–155.

    Article  PubMed  CAS  Google Scholar 

  • Hoffman, W.L., Jump, A.A. (1986): Tween 20 Removes Antibodies and Other Proteins from Nitrocellulose. J. Immunol. Methods 94, 191–196.

    Article  PubMed  CAS  Google Scholar 

  • Hoffman, W.L., Jump, A.A. (1989): Inhibition of the Streptavidin Biotin Interaction by Milk. Anal. Biochem. 181, 318–320.

    Article  PubMed  CAS  Google Scholar 

  • Hong, H.-Y., Yoo, G.-S., Choi, J.-K. (2000): Direct Blue 71 Staining of Proteins Bound to Blotting Membranes. Electrophoresis 21, 841–845.

    Article  PubMed  CAS  Google Scholar 

  • Jacobson, G., Kårsnäs, P. (1990): Important Parameters in Semi-Dry Electrophoretic Transfer. Electrophoresis 11, 46–52.

    Article  PubMed  CAS  Google Scholar 

  • Jagersten, C., Edstrom, A., Olsson, B., Jacobson, G. (1988): Blotting from PhastGel media after horizontal sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Electrophoresis 9, 662–665.

    Article  PubMed  CAS  Google Scholar 

  • Jahn, R., Schiebler, W., Greengard, P. (1984): A Quantitative Dot-Immunobinding Assay for Proteins Using Nitrocellulose MembraneFilters. Proc. Natl. Acad. Sci. USA 81, 1.684–1.687.

    Article  Google Scholar 

  • Jolly, C.L., Beisner, B.M., Holmes, I.H. (2000): Rotavirus Infection of MA104 Cells is Inhibited by Ricinus Lectin and Separately Expressed Single Binding Domains. Virology 275, 89–97.

    Article  PubMed  CAS  Google Scholar 

  • Karey, K.P., Sirbasku, D.A. (1989): Glutaraldehyde Fixation Increases Retention of Low Molecular Weight Proteins (Growth Factors) Transferred to Nylon Membranes for Western Blot Analysis. Anal. Biochem. 178, 255–259.

    Article  PubMed  CAS  Google Scholar 

  • Kemper, C., Berggren, K., Diwu, Z., Patton, W.F. (2001): An Improved, Luminescent Europium-Based Stain for Detection of Electroblotted Proteins on Nitrocellulose or Polyvinylidene Difluoride Membranes. Electrophoresis 22, 881–889.

    Article  PubMed  CAS  Google Scholar 

  • Koch, C., Skjødt, K., Laursen, I. (1985): A Simple Immunoblotting Method After Separation of Proteins in Agarose Gels. J. Immunol. Methods 84, 271–278.

    Article  PubMed  CAS  Google Scholar 

  • Kowit, J.D., Maloney, J. (1982): Protein Cleavage by Boiling in Sodium Dodecyl Sulfate Prior to Electrophoresis. Anal. Biochem. 123, 86–93.

    Article  PubMed  CAS  Google Scholar 

  • Kricka, L.J. (1993): Ultrasensitive Immunoassay Techniques. Clin. Biochem. 26, 325–331.

    Article  PubMed  CAS  Google Scholar 

  • Kubo, K. (1995): Effect of Incubation of Solutions of Proteins Containing Dodecyl Sulfate on the Cleavage of Peptide Bonds in Boiling. Anal. Biochem. 225, 351–353.

    Article  PubMed  CAS  Google Scholar 

  • Kyhse-Andersen, J. (1984): Electroblotting of Multiple Gels. A Simple Apparatus Without Buffer Tank for Rapid Transfer of Proteins from Polyacrylamide to Nitrocellulose. J. Biochem. Biophys. Methods 10, 203–209.

    Article  PubMed  CAS  Google Scholar 

  • Lauritzen, E., Masson, M., Rubin, I., Holm, A. (1990): Dot immunobinding and immunoblotting of picogram and nanogram quantities of small peptides on activated nitrocellulose. J. Immunol. Methods 131, 257–267.

    Article  PubMed  CAS  Google Scholar 

  • Lee, S.-K., Hacker, D.L. (2001): In vitro analysis of an RNA binding site within the N-terminal 30 amino acids of the southern cowpea mosaic virus coat protein. Virology 286, 317–327.

    Article  PubMed  CAS  Google Scholar 

  • Lobert, S., Correia, J.J. (1994): Method for rapid electrophoretic transfer of isoelectric focusing gels to polyvinylidene difluoride. Electrophoresis 15, 930–931.

    Article  PubMed  CAS  Google Scholar 

  • Mandrell, R.E., Zollinger, W.D. (1984): Use of Zwitterionic Detergent for the Restoration of Antibody-Binding Capacity of Electroblotted Meningococcal Outer Membrane Proteins. J. Immunol. Methods 67, 1–11.

    Article  PubMed  CAS  Google Scholar 

  • Matsudaira, P. (1987): Sequence from Picomole Quantities of Proteins Electroblotted onto Polyvinylidene Difluoride Membranes. J. Biol. Chem. 262, 10035–10038.

    PubMed  CAS  Google Scholar 

  • Mattson, D.L., Bellehumeur, T.G. (1996): Comparison of Three Chemiluminescent Horseradish Peroxidase Substrates for Immunoblotting. Anal. Biochem. 240, 306–308.

    Article  PubMed  CAS  Google Scholar 

  • McMahan, S.A., Burgess, R.R. (1996): Single-step synthesis and characterization of biotinylated nitrilotriacetic acid, a unique reagent for the detection of histidine-tagged proteins immobilized on nitrocellulose. Anal. Biochem. 236, 101–106.

    Article  PubMed  CAS  Google Scholar 

  • Moeremans, M., Daneels, G., De Mey, J. (1985): Sensitive Colloidal Metal (Gold or Silver) Staining of Protein Blots on Nitrocellulose Membranes. Anal. Biochem. 145, 315–321.

    Article  PubMed  CAS  Google Scholar 

  • Ochs, D. (1983): Protein Contaminants of Sodium Dodecyl Sulfate-Polyacrylamide Gels. Anal. Biochem. 135, 470–474.

    Article  PubMed  CAS  Google Scholar 

  • Otey, C.A., Kalnoski, M.H., Bulinski, J.C. (1986): A Procedure for the Immunoblotting of Proteins Separated on Isoelectric Focussing Gels. Anal. Biochem. 157, 71–76.

    Article  PubMed  CAS  Google Scholar 

  • Pasquali, C., Vilbois, F., Curchod, M.-L., van Huijsduijnen, R.H., Arigoni, F. (2000): Mapping and Identification of Protein-Protein Interactions by Two-Dimensional Far-Western Immunoblotting. Electrophoresis 21, 3357–3368.

    Article  PubMed  CAS  Google Scholar 

  • Peferoen, M., Huybrechts, R., De Loof, A. (1982): Vacuum-Blotting. A New Simple and Efficient Transfer of Proteins from Sodium Dodecyl Sulfate-Polyacrylamide Gels to Nitrocellulose. FEBS Lett. 145, 369–372.

    Article  CAS  Google Scholar 

  • Peluso, R.W., Rosenberg, G.H. (1987): Quantitative Electrotransfer of Proteins from Sodium Dodecyl Sulfate Polyacrylamide Gels onto Positively Charged Nylon Membranes. Anal. Biochem. 162, 389–398.

    Article  PubMed  CAS  Google Scholar 

  • Petersen, A. (2003): Two-Dimensional Electrophoresis Replica Blotting. A Valuable Technique for the Immunological and Biochemical Characterization of Single Components of Complex Extracts. Proteomics 3, 1206–1214.

    Article  PubMed  CAS  Google Scholar 

  • Rajan, N., Cao, Q., Anderson, B.E., Pruden, D.L., Sensibar, J., Duncan, J.L., Schaeffer, A.J. (1999): Roles of Glycoproteins and Oligosaccharides Found in Human Vaginal Fluid in Bacterial Adherence. Infect. Immun. 67, 5027–5032.

    PubMed  CAS  Google Scholar 

  • Ramlau, J. (1987): Use of Secondary Antibodies for Visualization of Bound Primary Reagents in Blotting Procedures. Electrophoresis 8, 398–402.

    Article  CAS  Google Scholar 

  • Rousset, E., Harel, J., Dubreuil, J.D. (1998): Sulfatide from the Pig Jejunum Brush Border Epithelial Cell Surface is Involved in Binding of Escherichia coli Enterotoxin B. Infect. Immun. 66, 5650–5658.

    PubMed  CAS  Google Scholar 

  • Sackett, D.L., Wolff, J. (1987): Nile Red as a Polarity-Sensitive Fluorescent Probe of Hydrophobic Protein Surfaces. Anal. Biochem. 167, 228–234.

    Article  PubMed  CAS  Google Scholar 

  • Salinovich, O., Montelaro, R.C. (1986): Reversible Staining and Peptide Mapping of Proteins Transferred to Nitrocellulose After Separation by Sodium Dodecylsulfate-Polyacrylamide Gel Electrophoresis. Anal. Biochem. 156, 341–347.

    Article  PubMed  CAS  Google Scholar 

  • Schapira, A.H., Keir, G. (1988): Two-Dimensional Protein Mapping by Gold Stain and Immunoblotting. Anal. Biochem. 169, 167–171.

    Article  PubMed  CAS  Google Scholar 

  • Schneppenheim, R., Budde, U., Dahlmann, U., Rautenberg, P. Method for Electrophoresis. Electrophoresis 12, 367–372.

    Google Scholar 

  • Scopsi, L., Larsson, L.I. (1986): Increased Sensitivity in Peroxidase Immunocytochemistry. A Comparative Study of a Number of Peroxidase Visualization Methods Employing a Model System. Histochemistry 84, 221–230.

    Article  PubMed  CAS  Google Scholar 

  • Seki, S., Akiyama, K., Watanabe, S., Tsutsui, K. (1993): Activity gel and Activity Blotting Methods for Detecting DNA-Modifying (Repair) Enzymes. J. Chromatogr. 618, 147–166.

    PubMed  CAS  Google Scholar 

  • Seshi, B. (1994): Cell Adhesion to Proteins Separated by Lithium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis and Blotted onto a Polyvinylidene Difluoride Membrane. A new Cell-Blotting Technique. J. Immunol. Methods 176, 185–201.

    Article  PubMed  CAS  Google Scholar 

  • Szewczyk, B., Kozloff, L.M. (1985): A Method for the Efficient Blotting of Strongly Basic Proteins from Sodium Dodecyl Sulfate-Polyacrylamide Gels to Nitrocellulose. Anal. Biochem. 150, 403–407.

    Article  PubMed  CAS  Google Scholar 

  • Tovey, E.R., Baldo, B.A. (1987): Comparison of Semi-Dry and Convenient Tank-Buffer Electrotransfer of Proteins from Polyacrylamide Gels to Nitrocellulose Membranes. Electrophoresis 8, 384–387.

    Article  CAS  Google Scholar 

  • Towbin, H., Staehelin, T., Gordon, J. (1979): Electrophoretic Transfer of Proteins from Polyacrylamide Gels to Nitrocellulose Sheets. Proc. Natl. Acad. Sci. USA 76, 4350–4354.

    Article  PubMed  CAS  Google Scholar 

  • Towbin, H., Staehelin, T., Gordon, J. (1989): Immunoblotting in the Clinical Laboratory. J. Clin. Chem. Clin. Biochem. 27, 495–501.

    PubMed  CAS  Google Scholar 

  • Van Seuningen, I., Davril, M. (1990): Electrotransfer of basic proteins from nondenaturing polyacrylamide acid gels to nitrocellulose: detection of enzymatic and inhibitory activities and retention of protein antigenicity. Anal. Biochem. 186, 306–311.

    Article  Google Scholar 

  • von Olleschik-Elbheim, L., el Bayâ, A., Schmidt, M.A. (1996): Quantification of immunological membrane reactions employing a digital desk top scanner and standard graphics software. J. Immunol. Methods 197, 181–186.

    Article  Google Scholar 

  • Weisburger, E.K., Russfield, A.B., Homburger, F., Weisburger, J.H., Boger, E., van Dongen, C.G., Chu, K.C. (1978): Testing of twenty-one environmental aromatic amines or derivatives for long-term toxicity or carcinogenicity. J. Environ. Pathol. Toxicol. 2, 325–356.

    PubMed  CAS  Google Scholar 

  • Wilchek, M., Bayer, E.A. (1988): The avidin-biotin complex in bioanalytical applications. Anal. Biochem. 171, 1–32.

    Article  PubMed  CAS  Google Scholar 

Literatur

  • Hames, B.D., Higgins, S.J. (1986): Nucleic Acid Hybridization, A Practical Approach. IRL Press, Oxford.

    Google Scholar 

  • Keller, G.H. (1989): DNA Probes. Stockten Press, New York.

    Google Scholar 

  • Sambrook, J., Russel, D.W. (2001): Molecular Cloning — A Laboratory Manual. 3rd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.

    Google Scholar 

  • The DIG System User’s Guide for Filter Hybridization (1995): Boehringer Mannheim GmbH Biochemica.

    Google Scholar 

  • Tijssen, P. (1994): Hybridization with Nucleic Acid Probes. Elsevier, Amsterdam.

    Google Scholar 

  • Wahl, G.M., Berger, S.L. (1987): Screening Colonies or Plaques with Radioactive Nucleic Acid Probes. Methods Enzymol. 152, 415–23.

    Article  PubMed  CAS  Google Scholar 

  • Wahl, G.M., Berger, S.L., Kimmel, A.R. (1987): Molecular Hybridization of Immobilized Nucleic Acids. Theoretical Concepts and Practical Considerations. Methods Enzymol. 152, 399–407.

    Article  PubMed  CAS  Google Scholar 

  • Wahl, G.M., Meinkoth, J.L., Kimmel, A.R. (1987): Northern and Southern Blots. Methods Enzymol. 152, 572–81.

    Article  PubMed  CAS  Google Scholar 

  • Wetmur, J. (1991): DNA Probes: Applications of the Principles of Nucleic Acid Hybridization. Crit. Rev. Biochem. Mol. Biol. 26, 227–259.

    Article  PubMed  CAS  Google Scholar 

Literatur

  • Costanzi, C., Gillespie, D. (1987): Fast Blots. Immobilization of DNA and RNA from Cells. Methods Enzymol. 152, 582–587.

    Article  PubMed  CAS  Google Scholar 

Literatur

  • Southern, E.M. (1975): Detection of Specific Sequences Among DNA Fragments Separated by Gel Electrophoresis. J. Mol. Biol. 98, 503–517.

    Article  PubMed  CAS  Google Scholar 

Literatur

  • Alwine, J.C. Kemp, D.J., Stark, G.R. (1977): Method for Detection of Specific RNAs in Agarose Gels by Transfer to Diazobenzyloxymethyl-Paper and Hybridization with DNA Probes. Proc. Natl. Acad. Sci. USA 74, 5.350–5.354.

    Article  Google Scholar 

  • Thomas, P.S. (1980): Hybridization of DenaturedRNAand Small DNA Fragments Transferred to Nitrocellulose. Proc. Natl. Acad. Sci. USA 77, 5.201–5.205.

    Article  Google Scholar 

Literatur

  • Grunstein, M., Hogness, D.S. (1975): Colony Hybridization. A Method for the Isolation of Cloned DNAs that Contain a Specific Gene. Proc. Natl. Acad. Sci. USA 72, 3.961–3.965.

    Article  Google Scholar 

  • Vogeli, G., Kaytes, P.S. (1987): Amplification, Storage and Replication of Libraries. Methods Enzymol. 152, 407–415.

    Article  PubMed  CAS  Google Scholar 

Literatur

  • Benton, W.D., Davis, R.W. (1977): Screening Lambda gt Recombinant Clones by Hybridization to Single Plaques In Situ. Science 196, 180–182.

    Article  PubMed  CAS  Google Scholar 

  • Davies, R.W. et al. (1980): Advanced Bacterial Genetics. Cold Spring Harbor, New York, 162–165 und 174–176.

    Google Scholar 

  • Huynh, T.V., Young, R.A., Davis, R.W. (1985) in: Glover, D.M. (Hrsg.): DNA Cloning, Volume 1. IRL Press, Oxford, 72–75.

    Google Scholar 

  • Vogeli, G., Kaytes, P.S. (1987): Amplification, Storage and Replication of Libraries. Methods Enzymol. 152, 407–415.

    Article  PubMed  CAS  Google Scholar 

Literatur

  • Denhardt, D.T. (1966): A Membrane-Filter Technique for the Detection of Complementary DNA. Biochem. Biophys. Res. Commun 23, 641.

    Article  PubMed  CAS  Google Scholar 

  • Hames, B.D., Higgins, S.J. (1986): Nucleic Acid Hybridization, A Practical Approach. IRL Press, Oxford.

    Google Scholar 

  • Keller, G.H. (1989): DNA Probes. Stockten Press. New York.

    Google Scholar 

  • McGinnis, W., Levine, M.S., Hafen, E., Kuroiwa, A., Gehring, W.J. (1984): A Conserved DNA Sequence in Homoeotic Genes of the Drosophila antennapedia and Bithorax Complexes. Nature 308, 428–433.

    Article  PubMed  CAS  Google Scholar 

  • Meinkoth, J., Wahl, G. (1984): Hybridization of Nucleic Acids Immobilized on Solid Supports. Anal. Biochem. 138, 267–284.

    Article  PubMed  CAS  Google Scholar 

  • Tijssen, P. (1994): Hybridization with Nucleic Acid Probes. Elsevier, Amsterdam, New York, Oxford.

    Google Scholar 

  • Wahl, G.M., Berger, S.L. (1987): Screening Colonies or Plaques with Radioactive Nucleic Acid Probes. Methods Enzymol. 152, 415–23.

    Article  PubMed  CAS  Google Scholar 

  • Wahl, G.M., Berger, S.L., Kimmel, A.R. (1987): Molecular Hybridization of Immobilized Nucleic Acids. Theoretical Concepts and Practical Considerations. Methods Enzymol. 152, 399–407.

    Article  PubMed  CAS  Google Scholar 

  • Wahl, G.M., Meinkoth, J.L., Kimmel, A.R. (1987): Northern and Southern Blots. Methods Enzymol. 152, 572–81.

    Article  PubMed  CAS  Google Scholar 

  • Wallace, R.B., Shaffer, J., Murphy, R.F., Bonner, J., Hirose, T., Itakura, K (1979): Hybridization of Synthetic Oligodeoxyribonucleotides to Phi Chi 174 DNA. The Effect of Single Base Pair Mismatch. Nucleic Acids Res. 6, 3.543–3.657.

    Article  Google Scholar 

  • Wetmur, J. (1991): DNA Probes: Applications of the Principles of Nucleic Acid Hybridization. Crit. Rev. Biochem. Mol. Biol. 26, 227–259.

    Article  PubMed  CAS  Google Scholar 

Literatur

  • Breslauer, K.J., Frank, R., Blocker, H., Markey, L.A. (1986): Predicting DNA Duplex Stability from the Base Sequence. Proc. Natl. Acad. Sci. USA 83, 3.746–3.750.

    Article  Google Scholar 

  • Keller, G.H. (1989): DNA Probes. Stockten Press. New York.

    Google Scholar 

  • Tijssen, P. (1994): Hybridization with Nucleic Acid Probes. Elsevier, Amsterdam.

    Google Scholar 

  • Wetmur, J. (1991): DNA Probes: Applications of the Principles of Nucleic Acid Hybridization. Crit. Rev. Biochem. Mol. Biol. 26, 227–259.

    Article  PubMed  CAS  Google Scholar 

Literatur

  • Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A., Struhl, K. (Hrsg.) (1987): Current Protocols in Molecular Biology. John Wiley & Sons, New York.

    Google Scholar 

  • Keller, G.H. (1989): DNA Probes. Stockten Press. New York.

    Google Scholar 

  • Nichols, R. et al. (1994): A Universal Nucleoside for Use at Ambiguous Sites in DNA Primers. Nature 369, 492–493.

    Article  PubMed  CAS  Google Scholar 

  • Sambrook, J., Fritsch, E.F., Maniatis, T. (1989): Molecular Cloning — A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.

    Google Scholar 

  • Suggs, S.V., Wallace, R.B., Hirose, T., Kawashima, E.H., Itaknra, K. (1981): Use of Synthetic Oligonucleotides as Hybridization Probes. Isolation of Cloned cDNA Sequences for Human Beta 2-Microglobulin. Proc. Natl. Acad. Sci. USA 78, 6.613–6.617.

    Article  Google Scholar 

  • The DIG System User’s Guide for Filter Hybridization (1995): Boehringer Mannheim GmbH Biochemica.

    Google Scholar 

  • Tijssen, P. (1994): Hybridization with Nucleic Acid Probes. Elsevier, Amsterdam, New York, Oxford.

    Google Scholar 

  • Wood, W.I. (1987): Gene Cloning Based on Long Oligonucleotide Probes. Methods Enzymol. 152, 443–447.

    Article  PubMed  CAS  Google Scholar 

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Monika Jansohn Sophie Rothhämel

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© 2012 Spektrum Akademischer Verlag Heidelberg

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Bade, S., Röckendorf, N., Frey, A., Petersen, A. (2012). Detektion von Protein und Nucleinsäure auf Membran. In: Jansohn, M., Rothhämel, S. (eds) Gentechnische Methoden. Spektrum Akademischer Verlag, Heidelberg. https://doi.org/10.1007/978-3-8274-2430-3_10

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