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Commercial Plant-Produced Recombinant Protein Products - Case Studies (Hardcover, 2014 ed.): John A. Howard, Elizabeth E. Hood Commercial Plant-Produced Recombinant Protein Products - Case Studies (Hardcover, 2014 ed.)
John A. Howard, Elizabeth E. Hood
R4,658 R3,374 Discovery Miles 33 740 Save R1,284 (28%) Ships in 12 - 17 working days

Attention has recently turned to using plants as hosts for the production of commercially important proteins. The twelve case studies in this volume present successful strategies for using plants to produce industrial and pharmaceutical proteins and vaccine antigens. They examine in detail projects that have commercial potential or products that have already been commercialized, illustrating the advantages that plants offer over bacterial, fungal or animal cell-culture hosts. There are many indications that plant protein production marks the beginning of a new paradigm for the commercial production of proteins that, over the next decade, will expand dramatically.

Plants as Factories for Protein Production (Hardcover, 2002 ed.): Elizabeth E. Hood, J.A. Howard Plants as Factories for Protein Production (Hardcover, 2002 ed.)
Elizabeth E. Hood, J.A. Howard
R4,306 Discovery Miles 43 060 Ships in 12 - 17 working days

For over 10 years, TMV -based vectors have been used as plant expression tools to examine gene regulation and function, protein processing, pathogen elicitors, to manipulate biosynthetic pathways, and to produce high levels of enzymes, proteins, or peptides of interest in different locations in a plant cell. TMV vectors often exhibit genetic stability of foreign RNA sequences through multiple passages in plant hosts. Foreign coding sequences can be expressed in plants where the stability, intracellular fate and enzymatic or biological activities of the recombinant proteins can be rapidly evaluated and optimized. These properties make viral vectors attracti ve expression vehicles for testing and production of a wide variety of recombinant peptides and proteins, for structural analyses of post-translational modifications and for assessing gene function and metabolic control. Finally, the utility of both CP fusion and dual subgenomic vectors has extended beyond the laboratory and greenhouse to field-scale production and purification of recombinant products for commercial use (Grill, 1992; Grill, 1993; Turpen et at. , 1997). REFERENCES Copeman RJ, Hartman IR and Watterson IC. 1969. Tobacco mosaic virus in inoculated and systemically infected tobacco leaves. Phytopathology 59: 1012-1013. Dawson WO, Beck DL, Knorr DA and Grantham GL. 1986. cDNA cloning of the complete genome of tobacco mosaic virus and production of infectious transcripts. Proc. Natl. Acad. Sci. (USA) 83: 1832-1836. Dawson WO and Lehto KM. 1990. Regulation of tobamovirus gene expression. Ad. Virus Res. 38:307-342. Dawson WOo 1992. Tobamovirus-Plant Interactions. Virology 186:359-367.

Commercial Plant-Produced Recombinant Protein Products - Case Studies (Paperback, Softcover reprint of the original 1st ed.... Commercial Plant-Produced Recombinant Protein Products - Case Studies (Paperback, Softcover reprint of the original 1st ed. 2014)
John A. Howard, Elizabeth E. Hood
R3,586 Discovery Miles 35 860 Ships in 10 - 15 working days

Attention has recently turned to using plants as hosts for the production of commercially important proteins. The twelve case studies in this volume present successful strategies for using plants to produce industrial and pharmaceutical proteins and vaccine antigens. They examine in detail projects that have commercial potential or products that have already been commercialized, illustrating the advantages that plants offer over bacterial, fungal or animal cell-culture hosts. There are many indications that plant protein production marks the beginning of a new paradigm for the commercial production of proteins that, over the next decade, will expand dramatically.

Plants as Factories for Protein Production (Paperback, Softcover reprint of hardcover 1st ed. 2002): Elizabeth E. Hood, J.A.... Plants as Factories for Protein Production (Paperback, Softcover reprint of hardcover 1st ed. 2002)
Elizabeth E. Hood, J.A. Howard
R4,207 Discovery Miles 42 070 Ships in 10 - 15 working days

For over 10 years, TMV -based vectors have been used as plant expression tools to examine gene regulation and function, protein processing, pathogen elicitors, to manipulate biosynthetic pathways, and to produce high levels of enzymes, proteins, or peptides of interest in different locations in a plant cell. TMV vectors often exhibit genetic stability of foreign RNA sequences through multiple passages in plant hosts. Foreign coding sequences can be expressed in plants where the stability, intracellular fate and enzymatic or biological activities of the recombinant proteins can be rapidly evaluated and optimized. These properties make viral vectors attracti ve expression vehicles for testing and production of a wide variety of recombinant peptides and proteins, for structural analyses of post-translational modifications and for assessing gene function and metabolic control. Finally, the utility of both CP fusion and dual subgenomic vectors has extended beyond the laboratory and greenhouse to field-scale production and purification of recombinant products for commercial use (Grill, 1992; Grill, 1993; Turpen et at. , 1997). REFERENCES Copeman RJ, Hartman IR and Watterson IC. 1969. Tobacco mosaic virus in inoculated and systemically infected tobacco leaves. Phytopathology 59: 1012-1013. Dawson WO, Beck DL, Knorr DA and Grantham GL. 1986. cDNA cloning of the complete genome of tobacco mosaic virus and production of infectious transcripts. Proc. Natl. Acad. Sci. (USA) 83: 1832-1836. Dawson WO and Lehto KM. 1990. Regulation of tobamovirus gene expression. Ad. Virus Res. 38:307-342. Dawson WOo 1992. Tobamovirus-Plant Interactions. Virology 186:359-367.

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