Therapeutic Proteins Methods and Protocols /
With the completion of the human genome, the number of protein-based drug candidates has increased dramatically, along with the need to find methods for producing these proteins on a scale large enough to meet demand without compromising the authenticity of the final product. In Therapeutic Proteins...
שמור ב:
| מחבר תאגידי: | |
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| מחברים אחרים: | , |
| פורמט: | אלקטרוני ספר אלקטרוני |
| שפה: | English |
| יצא לאור: |
Totowa, NJ :
Humana Press : Imprint: Humana,
2005.
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| מהדורה: | 1st ed. 2005. |
| סדרה: | Methods in Molecular Biology,
308 |
| נושאים: | |
| גישה מקוונת: | https://doi.org/10.1385/1592599222 |
| תגים: |
הוספת תג
אין תגיות, היה/י הראשונ/ה לתייג את הרשומה!
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תוכן הענינים:
- Biopharmaceutical Proteins
- Expression of Antibody Fragments by Periplasmic Secretion in Escherichia coli
- Secretory Production of Therapeutic Proteins in Escherichia coli
- Expression of Recombinant LTB Protein in Marine vibrio VSP60
- Heterologous Gene Expression in Yeast
- Pharmaceutical Proteins From Methylotrophic Yeasts
- Expression of Human Papillomavirus Type 16 L1 in Baculovirus Expression Systems
- Large-Scale Transient Expression of Therapeutic Proteins in Mammalian Cells
- Site-Specific Integration for High-Level Protein Production in Mammalian Cells
- Production of Recombinant Therapeutic Proteins by Mammalian Cells in Suspension Culture
- Transgene Control Engineering in Mammalian Cells
- Fusion to Albumin as a Means to Slow the Clearance of Small Therapeutic Proteins Using the Pichia pastoris Expression System
- High-Throughput Recovery of Therapeutic Proteins from the Inclusion Bodies of Escherichia coli
- Isolation, Solubilization, Refolding, and Chromatographic Purification of Human Growth Hormone from Inclusion Bodies of Escherichia coli Cells
- Large-Scale Preparation of Factor VIIa from Human Plasma
- Purification of Clinical-Grade Monoclonal Antibodies by Chromatographic Methods
- Virus Elimination and Validation
- Virus Removal by Nanofiltration
- Determining Residual Host Cell Antigen Levels in Purified Recombinant Proteins by Slot Blot and Scanning Laser Densitometry
- Principles of Biopharmaceutical Protein Formulation
- Solid-State Protein Formulation
- Stabilization of Therapeutic Proteins by Chemical and Physical Methods
- Extraction and Characterization of Vaccine Antigens from Water-in-Oil Adjuvant Formulations
- Probing Reversible Self-Association of Therapeutic Proteins by Sedimentation Velocity in the Analytical Ultracentrifuge
- Biological Characterization of Pegylated Interferons
- Characterization of Interferon ?2B Pegylated via Carboxyalkylation
- Quantifying Recombinant Proteins and Their Degradation Products Using SDS-PAGE and Scanning Laser Densitometry
- Extraction and Denaturing Gel Electrophoretic Methodology for the Analysis of Yeast Proteins
- Characterization of Therapeutic Proteins by Membrane and In-Gel Tryptic Digestion
- Oligosaccharide Release and MALDI-TOF MS Analysis of N-Linked Carbohydrate Structures from Glycoproteins
- Capillary Electrophoresis of Carbohydrates Derivatized With Fluorophoric Compounds
- High-Throughput LC/MS Methodology for ?(1?3)Gal Determination of Recombinant Monoclonal Antibodies
- Carbohydrate Structural Characterization of Fas Ligand Inhibitory Protein
- Top-Down Characterization of Protein Pharmaceuticals by Liquid Chromatography/Mass Spectrometry
- Sample Preparation Procedures for High-Resolution Nuclear Magnetic Resonance Studies of Aqueous and Stabilized Solutions of Therapeutic Peptides.