Recombinant proteins from plants : production and isolation of clinically useful compounds
Author(s)
Bibliographic Information
Recombinant proteins from plants : production and isolation of clinically useful compounds
（Methods in biotechnology, 3）
Humana Press, c1998
Available at 10 libraries
Note
Includes bibligraphical references and index
Description and Table of Contents
Description
Recombinant Proteins from Plants is one of the most exciting and fastest developing areas in biology. The latest molecular techniques are being applied to the exploitation of plants as novel expression systems for the p- duction and overproduction of heterologous and native proteins. Transgenic plant technology is currently used in three broad areas: the expression of - combinant proteins to improve crop quality by increasing disease/pest res- tance or increasing tolerance to stress, optimizing plant productivity and yield by the genetic manipulation of metabolic pathways, and the large-scale co- effective production of recombinant proteins for use as specialist industrial or therapeutic biomolecules. The intention of Recombinant Proteins from Plants is to provide c- prehensive and detailed protocols covering all the latest molecular approaches. Because the production oftransgenic plants has become routine in many la- ratories, coverage is also given to some of the more "classical" approaches to the separation, analysis, and characterization of recombinant proteins. The book also includes areas of research that we believe will become increasingly important in the near future: efficient transformation of monocots with Agrobacterium optimizing the stability of recombinant proteins, and a section highlighting the immunotherapeutic potential of plant-expressed proteins.
Table of Contents
Rice Transformation by Agrobacterium Infection, X. Cheng, R. K. Sardana, and I. Altosaar. Barley as a Producer of Heterologous Protein, L. Mannonen, K. Aspegren, A. Ritala, H. Simola, and T. H. Teeri. Introducing and Expressing Genes in Legumes, A. D. Bavage, M. P. Robbins, L. Skot, and K. J. Webb. Use of the GUS Reporter Gene, J. Wilkinson and K. Lindsey. Expression of Recombinant Proteinase Inhibitors in Plants, D. Michaud and T. C. Vrain. Detection of Recombinant Viral Coat Protein in Transgenic Plants, H. Steinkellner and I. Korschineck. Synthesis of Recombinant Human Cytokine GM-CSF in the Seeds of Transgenic Tobacco Plants, R. K. Sardana, P. R. Ganz, A. Dudani, E. S. Tackaberry, X. Cheng, and I. Altosaar. Tobamovirus Vectors for Expression of Recombinant Genes in Plants, T. H. Turpen and S. J. Reinl. Single-Chain Fv Antibodies Expressed in Plants, U. Conrad, U. Fiedler, O. Artsaenko, and J. Phillips. Characterization and Applications of Plant-Derived Recombinant Antibodies, R. Fischer, J. Drossard, Y. Liao, and S. Schillberg. Production of Recombinant Antibodiesin Plant Suspension Cultures, J. Drossard, Y.-C. Liao, and R. Fischer. Production of Foreign Proteins in Tobacco Cell Suspension Culture, V. Gomord, A.-C. Fitchette-Laine, L.-A. Denmat, D. Michaud, and L. Faye. Transient Gene Expression in Plant Protoplasts, S. Schillberg, S. Zimmermann, D. Prufer, D. Schuman, and R. Fischer. Stability of Recombinant Proteins in Plants, D. Michaud, T. C. Vrain, V. Gomord, and L. Faye. Trafficking and Stability of Heterologous Proteinsin Transgenic Plants, J. A. Napier, G. Richard, and P. R. Shewry. Screening for Transgenic Lines with Stableand Suitable Accumulation Levels of a Heterologous Protein, M. De Neve, H. Van Houdt, A.-M. Bruyns, M. Van Montagu, and A. Depicker. Manipulation of Photosynthetic Metabolism, M. A. J. Parry, S. P. Colliver, P. J. Madgwick, and M. J. Paul. Quantification of Heterologous Protein Levelsin Transgenic Plants by ELISA, A.-M. Bruyns, M.De Neve, G. De Jaeger, C. De Wilde, P. Rouze, and A. Depicker. Analysis of N- and O-Glycosylation of Plant Proteins, A.-C. Fitchette-Laine, L.-A. Denmat, P. Lerouge, and L. Faye. Two-Dimensional Electrophoresis: A Tool for Protein Separation and Processing for Microsequencing, N. P. E. Reddy and M. Jacobs. Index.
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