Intro -- Proteins: Biochemistry and Biotechnology -- Copyright -- Contents -- Preface -- About the companion website -- Chapter 1 Proteins and proteomics -- 1.1 Proteins, an introduction -- 1.2 Genes, genomics and proteomics -- 1.2.1 Electrophoresis -- 1.2.2 High-pressure liquid chromatography -- 1.2.3 Mass spectrometry -- 1.3 Bioinformatics -- 1.4 Proteomics: goals and applications -- 1.4.1 Expression proteomics -- 1.4.2 Functional proteomics -- 1.4.3 Structural proteomics -- Further reading -- Chapter 2 Protein structure and engineering -- 2.1 Primary structure -- 2.1.1 The peptide bond -- 2.1.2 Amino acid sequence determination -- 2.1.3 Bioinformatic analysis of sequence data -- 2.2 Higher-level structure -- 2.2.1 Secondary structure -- 2.2.2 Tertiary structure -- 2.3 Protein classification on the basis of structure -- 2.3.1 Higher structure determination -- 2.4 Protein structural stability -- 2.5 Higher-order structure prediction -- 2.5.1 Secondary structure prediction -- 2.5.2 Tertiary structure prediction -- 2.6 Protein folding -- 2.7 Intrinsically disordered proteins -- 2.8 Protein engineering -- 2.8.1 Site-directed mutagenesis -- 2.8.2 Directed evolution -- 2.9 Protein post-translational modification -- 2.9.1 Glycosylation -- 2.9.2 Proteolytic processing -- 2.9.3 Phosphorylation -- 2.9.4 Acetylation, acylation and amidation -- 2.9.5 Sulfation -- 2.9.6 PTM engineering -- 2.9.7 Protein PEGylation -- Further reading -- Chapter 3 Protein sources -- 3.1 Recombinant versus non-recombinant production -- 3.2 Approaches to recombinant protein production -- 3.3 Heterologous protein production in E. coli -- 3.3.1 Inclusion body formation -- 3.3.2 Extracellular production -- 3.3.3 Other characteristics of heterologous protein production in E. coli -- 3.4 Heterologous production in bacteria other than E. coli.

3.5 Heterologous protein production in yeast -- 3.6 Heterologous protein production in fungi -- 3.7 Proteins from plants -- 3.7.1 Production of heterologous proteins in plants -- 3.8 Animal tissue as a protein source -- 3.9 Heterologous protein production in transgenic animals -- 3.10 Heterologous protein production using animal cell culture -- 3.11 Insect cell culture systems -- Further reading -- Chapter 4 Protein purification and characterization -- 4.1 Protein detection and quantification -- 4.2 Initial recovery of protein -- 4.2.1 Cell disruption: animal and plant cells -- 4.2.2 Microbial cell disruption -- 4.3 Removal of whole cells and cell debris -- 4.3.1 Centrifugation -- 4.3.2 Filtration -- 4.3.3 Aqueous two-phase partitioning -- 4.3.4 Removal of nucleic acid and lipid -- 4.4 Concentration -- 4.4.1 Concentration by precipitation -- 4.4.2 Concentration by ion exchange -- 4.4.3 Concentration by ultrafiltration -- 4.4.4 Diafiltration -- 4.5 Chromatographic purification -- 4.5.1 Size exclusion chromatography (gel filtration) -- 4.5.2 Ion-exchange chromatography -- 4.5.3 Hydrophobic interaction chromatography -- 4.5.4 Affinity chromatography -- 4.5.5 Chromatography on hydroxyapatite -- 4.5.6 Chromatofocusing -- 4.5.7 High performance liquid chromatography -- 4.5.8 Purification of recombinant proteins -- 4.5.9 Purification of membrane proteins -- 4.6 Protein inactivation and stabilization -- 4.6.1 Chemical inactivation -- 4.6.2 Inactivation by biological or physical influences -- 4.6.3 Approaches to protein stabilization -- 4.6.4 Protein drying -- 4.7 Protein characterization -- 4.7.1 Functional studies -- Further reading -- Chapter 5 Large-scale protein production -- 5.1 Upstream processing -- 5.1.1 Cell line development -- 5.1.2 Cell banking systems -- 5.1.3 Microbial cell fermentation -- 5.1.4 Mammalian cell culture.

5.2 Downstream processing -- 5.2.1 Scale-up of protein purification -- 5.2.2 Downstream processing scale-up: bioprocess engineering aspects -- 5.2.3 Bulk protein production -- 5.2.4 Purification of proteins used for therapeutic or analytical purposes -- 5.3 Therapeutic protein production: some special issues -- 5.3.1 Clean areas -- 5.3.2 Cleaning, decontamination and sanitation -- 5.4 Range and medical significance of impurities potentially present in protein-based therapeutic products -- 5.4.1 Microbial and viral contaminants -- 5.4.2 Pyrogenic contaminants -- 5.4.3 DNA contaminants -- 5.4.4 Protein contaminants -- 5.4.5 Chemical and miscellaneous contaminants -- 5.4.6 Labelling and packing of finished products -- Further reading -- Chapter 6 Therapeutic proteins: blood products, vaccines and enzymes -- 6.1 Blood products -- 6.1.1 Whole blood and blood plasma -- 6.1.2 Blood-derived proteins -- 6.2 Anticoagulants -- 6.2.1 Traditional anticoagulants -- 6.2.2 Hirudin -- 6.2.3 Antithrombin -- 6.3 Thrombolytic agents -- 6.3.1 The fibrinolytic system -- 6.3.2 Tissue plasminogen activator-based products -- 6.4 Additional blood-related products -- 6.4.1 Human serum albumin -- 6.4.2 (Sa(B 1 -Antitrypsin -- 6.5 Vaccine technology -- 6.5.1 The impact of genetic engineering on vaccine technology -- 6.5.2 Cancer vaccines -- 6.5.3 Vaccine vectors -- 6.6 Therapeutic enzymes -- 6.6.1 Asparaginase -- 6.6.2 Debriding and anti-inflammatory agents -- 6.6.3 Enzymes as digestive aids -- 6.6.4 Enzymes produced by recombinant means -- Further reading -- Chapter 7 Therapeutic antibodies -- 7.1 Antibodies -- 7.2 IgG structure and activity -- 7.3 Antibody therapeutics: polyclonal antibody preparations -- 7.4 Antibody therapeutics: monoclonal antibodies -- 7.4.1 Hybridoma technology -- 7.4.2 Overcoming the limitations of murine monoclonal antibodies.

7.4.3 Chimeric and humanized antibodies -- 7.4.4 Fully human monoclonal antibodies -- 7.4.5 Purification of therapeutic monoclonal antibodies -- 7.5 Therapeutic applications of monoclonal antibodies -- 7.5.1 Monoclonal antibody-mediated antigen neutralization -- 7.5.2 Monoclonal antibody-mediated cell destruction -- 7.6 Antibody conjugates -- 7.6.1 Radiolabelled antibody conjugates -- 7.6.2 Antibody-toxin conjugates -- 7.6.3 Antibody-enzyme conjugates -- 7.7 Bispecific antibodies -- 7.8 Antibody fragments -- 7.9 Engineering the antibody glycocomponent -- 7.10 Fc fusion proteins -- Further reading -- Chapter 8 Hormones and growth factors used therapeutically -- 8.1 Insulin -- 8.1.1 Type 1 diabetes -- 8.1.2 Insulin synthesis in vivo -- 8.1.3 The industrial production of insulin -- 8.1.4 Insulin production by recombinant means -- 8.1.5 Insulin formulations -- 8.1.6 Engineered insulins -- 8.2 Glucagon -- 8.3 Gonadotrophins -- 8.3.1 FSH, LH and hCG -- 8.3.2 Sources of FSH, LH and hCG -- 8.4 Growth hormone -- 8.5 Erythropoietin -- 8.6 Other hormones -- 8.7 Growth factors -- 8.7.1 Colony-stimulating factors -- 8.7.2 Production and medical applications of CSFs -- 8.7.3 Some additional growth factors -- Further reading -- Chapter 9 Interferons, interleukins and tumour necrosis factors -- 9.1 Regulatory factors: cytokines versus hormones -- 9.2 Interferons -- 9.2.1 Interferon (Sa(B -- 9.2.2 Interferon (Sb(B -- 9.2.3 Interferon (Sd(B -- 9.2.4 Production and medical applications of IFN - (Sa(B -- 9.2.5 Production and medical applications of IFN - (Sb(B -- 9.2.6 Production and medical uses of IFN - (Sd(B -- 9.3 Interleukins -- 9.3.1 Interleukin-2 -- 9.3.2 Interleukin-11 -- 9.3.3 Interleukin-1 -- 9.4 Tumour necrosis factors -- 9.4.1 TNF - (Sa(B -- Further reading -- Chapter 10 Proteins used for analytical purposes -- 10.1 The IVD sector.

10.2 The basis of analyte detection and quantification -- 10.3 Enzymes as diagnostic/analytical reagents -- 10.3.1 End-point versus kinetic methods -- 10.3.2 Some common ­enzyme-based diagnostic tests -- 10.3.3 Assay of blood glucose -- 10.3.4 Assay of blood cholesterol and triglycerides -- 10.3.5 Assay of blood urea and uric acid -- 10.3.6 Immobilized enzymes as diagnostic reagents -- 10.4 Biosensors -- 10.4.1 Enzyme-based biosensors -- 10.4.2 Non-enzyme-based biosensors -- 10.5 Antibodies as analytical reagents -- 10.5.1 Classical immunoassay systems -- 10.5.2 Fluorescent and chemiluminescent-based immunoassay labels -- 10.5.3 Latex agglutination-based immunoassay formats -- 10.5.4 Membrane-bound diagnostic systems -- Further reading -- Chapter 11 Industrial enzymes: an introduction -- 11.1 Sales value and manufacturers -- 11.2 Sources and engineering -- 11.3 Environmental benefits -- 11.4 Enzyme detection and quantification -- 11.5 Immobilized enzymes -- 11.5.1 Gel/fibre entrapment -- 11.5.2 Immobilization via adsorption -- 11.6 Extremophiles -- 11.6.1 Hyperthermophiles -- 11.6.2 Thermoacidophiles and their enzymes -- 11.6.3 Enzymes from additional extremophiles -- 11.7 Enzymes in organic solvents -- 11.8 Industrial enzymes: the future -- Further reading -- Chapter 12 Industrial enzymes: proteases and carbrohydrases -- 12.1 Proteolytic enzymes -- 12.1.1 Classification of proteases -- 12.1.2 Detergent proteases -- 12.1.3 Proteases used in cheese manufacture -- 12.1.4 Proteases and meat tenderization -- 12.1.5 Proteases and leather production -- 12.1.6 Synthesis of aspartame -- 12.1.7 Protease enzymes used in the brewing and baking industries -- 12.1.8 Enzymatic conversion of protein waste -- 12.2 Carbohydrases -- 12.2.1 Amylases -- 12.2.2 Lignocellulose-degrading enzymes -- 12.2.3 Pectin and pectic enzymes -- Further reading.

Chapter 13 Additional industrial enzymes.

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Electronic reproduction. Ann Arbor, Michigan : ProQuest Ebook Central, 2022. Available via World Wide Web. Access may be limited to ProQuest Ebook Central affiliated libraries.