Post-translational modification of protein biopharmaceuticals:
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2009
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| Beschreibung: | XIX, 370 S. Ill., graph. Darst. |
| ISBN: | 9783527320745 |
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| 245 | 1 | 0 | |a Post-translational modification of protein biopharmaceuticals |c ed. by Gary Walsh |
| 264 | 1 | |a Weinheim |b Wiley-VCH |c 2009 | |
| 300 | |a XIX, 370 S. |b Ill., graph. Darst. | ||
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| 650 | 4 | |a Biopharmaceutics |x methods | |
| 650 | 4 | |a Biotechnology |x methods | |
| 650 | 4 | |a Glycosylation | |
| 650 | 4 | |a Pharmaceutical biotechnology | |
| 650 | 4 | |a Post-translational modification | |
| 650 | 4 | |a Protein Engineering |x methods | |
| 650 | 4 | |a Protein Processing, Post-Translational | |
| 650 | 4 | |a Proteins |x analysis | |
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Datensatz im Suchindex
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Titel: Post-translational modification of protein biopharmaceuticals
Autor: Walsh, Gary
Jahr: 2009
Contents
Preface XV
List of Contributors XVII
1 Post-Translational Modifications in the Context of Therapeutic
Proteins: An Introductory Overview 1
Gary Walsh
1.1 Introduction 1
1.2 Biopharmaceuticals and the Biopharmaceutical Sector 1
1.3 Protein Post-Translational Modification 2
1.4 PTMs in the Context of Biopharmaceuticals 7
1.5 Some Specific PTMs 8
1.5.1 Glycosylation 8
1.5.2 Disulfide Bond Formation and Proteolytic Cleavage 10
1.5.3 y-Carboxylation and P-Hydroxylation 11
1.5.4 Amidation and Sulfation 12
1.6 Extending and Engineering PTM Profiles 12
1.7 Conclusion 13
References 14
Part One Glycosylation 15
2 Protein Glycosylation: The Basic Science 17
Susan A. Brooks
2.1 Introduction - Glycosylated Proteins 17
2.2 Basic Building Blocks of Glycosylation in Human Cells 18
2.3 Formation of Complex Glycan Structures 19
2.3.1 a and p Glycosidic Bonds 19
2.3.2 Structural Complexity of Glycoprotein Glycans 19
2.4 Glycan Synthesis is Catalyzed by Enzymes of Glycosylation - the
"Glycozymes" 22
Post-translational Modification of Protein Biopharmaceuticals. Edited by Gary Walsh
Copyright © 2009 WILEY-VCH Verlag GmbH Co. KGaA, Weinheim
ISBN: 978-3-527-32074-5
VI Contents
2.5 Protein Glycosylation - Relationship Between N-linked and O-linked
Glycoproteins 23
2.6 N-linked Glycoproteins 24
2.6.1 Where Does N-linked Glycosylation of Proteins Take Place? 24
2.6.2 Why is it Called N-linked? 24
2.6.3 N-Glycosylation Step-by-Step 24
2.6.3.1 Polypeptide Enters the RER 24
2.6.3.2 Building and Positioning the Dolichol Oligosaccharide Precursor 24
2.6.3.3 Attachment of the Dolichol Oligosaccharide Precursor to the
Polypeptide Chain 25
2.6.3.4 Trimming the Dolichol Oligosaccharide Precursor in the RER 25
2.6.3.5 Processing of N-linked Oligosaccharides in the Golgi Apparatus 25
2.6 A Three Classes of N-linked Glycoproteins 25
2.6.5 What Determines Whether a Potential Site of N-Glycosylation on
the Polypeptide Chain is Occupied or Not? 27
2.7 O-linked Glycoproteins 27
2.7.1 Why is it Called O-linked? 28
2.7.2 Different Types of O-linked Glycosylation 28
2.7.3 Overview of O-linked Mucin-Type Protein Glycosylation 28
2.7A No Consensus Sequence for Mucin-Type O-linked Glycoprotein
Glycosylation 29
2.7.5 Synthesis of O-linked Mucin-Type Glycan Core Structures
Step-by-Step 29
2.7.5.1 Initiation - Synthesis of GalNAcod^ Ser/Thr (Tn Epitope) 29
2.7.5.2 Synthesis of NeuNAc(a2-^6)GalNAcat^Ser/Thr (Sialyl Tn) 29
2.7.5.3 Synthesis of Core 1, Gal(P1^3)GalNAcoc-Ser/Thr, or the
Thomsen-Friedenreich (T or TF) Antigen 29
2.7.5.4 Synthesis of Core 2, GlcNAc(Rl-*6)[GalR(l-+3)]GalNAcal-Ser/
Thr 31
2.7.5.5 Synthesis of Core 3, GlcNAc(pi^3)GalNAcal-^Ser/Thr 31
2.7.5.6 Synthesis of Core 4, GkNAc((31^ 6)[GlcNAc(pl-+ 3)]
GalNAcotl-Ser/Thr 31
2.7.5.7 Less Common Core Structures 31
2.7.6 Regulation of O-Glycan Synthesis 32
2.8 O- and N-linked Glycan Chain Extension and Commonly Occurring
Glycan Motifs 32
2.8.1 Type I Chains or Neolactosamine Units, Gal(pi^3)GlcNAc/
GalNAc 32
2.8.2 Type 2 Chains or Lactosamine Units, Gal(pi^4)GlcNAc 33
2.8.3 Termination of Glycan Chains 33
2.8.4 Blood Group Antigens 33
2.9 Analytical Methodologies Developed to Detect and Characterize
Glycosylation 33
2.9.1 Glycan Analysis is Complex and Requires a Number of
Techniques 33
Contents VII
2.9.2 Detection of Glycans 34
2.9.2.1 Periodic Acid-Schiff (PAS) Reaction 34
2.9.2.2 Recognition Through Lectin Binding 34
2.9.2.3 Pulsed Amperometric Detection (PAD) of Unlabelled
Free Glycans 35
2.9.2.4 Labeling Glycans with Radiolabels or Fluorescent Labels 35
2.9.3 Profiling Glycans Using Microarrays 35
2.9.4 One- and Two-Dimensional Gel Electrophoresis - Exploring the
Glycome 36
2.9.5 Chemical Release and Analysis of Monosaccharides 36
2.9.6 Chemical Release of Intact Oligosaccharides 37
2.9.7 Enzymatic Release of Intact Oligosaccharides 37
2.9.8 Sequential Exoglycosidase Digestions to Provide Monosaccharide
Sequence and Linkage Data 37
2.9.9 Oligosaccharide Separation and Mapping by High-Performance
Liquid Chromatography (HPLC) 38
2.9.9.1 Normal Phase HPLC (NP-HPLC) 38
2.9.9.2 Weak Anion Exchange High-Performance Liquid Chromatography
(WAX-HPLC) 38
2.9.9.3 High-Performance (or High pH) Anion Exchange Chromatography
(HPAEC) 39
2.9.10 Separation and Mapping of Oligosaccharides by Fluorophore-Assisted
Carbohydrate Electrophoresis (FACE) 39
2.9.11 Separation and Mapping of Oligosaccharides by Capillary
Electrophoresis (CE) 39
2.9.12 Oligosaccharide Analysis by Nuclear Magnetic Resonance (NMR) 40
2.9.13 Determining the Mass of an Oligosaccharide Using Mass
Spectrometry (MS) 40
2.9.14 Gas-liquid Chromatography (GLQ/MS for Determining the Linkage
Position of Monosaccharides in Oligosaccharides 41
2.10 Conclusion 42
References 42
3 Mammalian Cell Lines and Glycosylation: A Case Study 51
Michael Butler
3.1 Introduction 51
3.2 The Choice of Cell line for Glycoprotein Production 53
3.3 Effect of Growth and Protein Production Rate on Glycosylation 54
3.4 Enzymes Associated with Glycan Heterogeneity 55
3.4.1 N-Acetyl Glucosaminyltransferases 55
3.4.2 Fucosylation 57
3.4.3 Sialylation 58
3.5 Immunogenicity of Non-Human Glycans 61
3.6 Culture Parameters that may Affect Glycosylation 61
3.6.1 Nutrient Depletion 61
VIII Contents
3.6.2 Fed-Batch Cultures and Supplements 63
3.6.2.1 Glucosamine as a Supplement 64
3.6.2.2 Galactose as a Supplement 65
3.6.3 Ammonia 65
3.6.4 pH 66
3.6.5 Oxygen 66
3.7 Functional Glycomics 67
3.8 Conclusion 68
References 69
4 Antibody Clycosylation 79
Royjefferis
4.1 Introduction 79
4.2 Antibodies 80
4.2.1 Basic Structure/Function 80
4.2.2 Antibody (Immunoglobulin) Isotypes 84
4.3 Glycosylation 84
4.3.1 Glycosylation of Normal Human IgG 84
4.3.2 Impact of Glycosylation on Structure 86
4.3.3 Impact of Glycosylation on Stability 87
4.4 IgG-Fc Effector Functions 88
4A.I Inflammatory Cascades 88
4.4.2 Catabolism, Pharmacokinetics and Placental Transport 90
4.5 Individual IgG-Fc Glycoforms 91
4.5.1 Individual IgG-Fc Glycoforms and Effector Activities 92
4.5.2 Sialylation of IgG-Fc Oligosaccharides 92
4.5.3 Influence of Galactosylation on IgG-Fc Activities 92
4.5.4 Influence of Fucose and Bisecting N-Acetylglucosamine on IgG-Fc
Activities 94
4.6 IgG-Fab Glycosylation 96
4.7 Recombinant Monoclonal Antibodies for Therapy 98
4.8 Conclusions and Future Perspectives 100
References 100
5 Gonadotropins and the Importance of Clycosylation 109
Alfredo Ulloa-Aguirre, James A. Dias, and George R. Bousfield
5.1 Introduction 109
5.2 Structure of Gonadotropins 111
5.3 Glycosylation of Gonadotropins and Structural
Microheterogeneity 114
5.4 Role of Glycosylation in the Function of Gonadotropins 121
5.4.1 Role in Folding, Subunit Assembly and Secretion 121
5.4.2 Metabolic Clearance Rate 122
5.4.3 Binding and Signal Transduction 123
5.4.4 LH and FSH Glycoforms and Gonadorropin Function 124
Contents IX
5.4.5 Chorionic Gonadotropin Glycoforms and Function 126
5.5 Regulation of Gonadotropin Glycosylation 127
5.5.1 Effects of Estrogens 127
5.5.2 Effects of Androgens 228
5.5.3 Effects of Gonadotropin-Releasing Hormone 129
5.6 Therapeutic Applications of Gonadotropins 130
5.7 Conclusions 132
References 133
6 Yeast Glycosylation and Engineering in the Context of
Therapeutic Proteins 149
Terrance A. Stadheim and Natarajan Sethuraman
6.1 Introduction 149
6.2 N-Glycosylation in Fungi 150
6.3 O-Glycosylation in Fungi and Mammals 152
6.4 Remodeling Yeast Glycosylation for Therapeutic Protein
Production 154
References 160
7 Insect Cell Glycosylation Patterns in the Context of
Biopharmaceuticals 265
Christoph Ceislerand Donjarvis
7.1 Introduction 265
7.2 Recombinant N-Glycoproteins in the BEVS Product Pipeline 266
7.2.1 Chimigen® Vaccines 267
7.2.2 FluBlok® 267
7.2.3 Influenza Virus-Like Particles 267
7.2.4 Provenge® 267
7.2.5 Specifid® 268
7.3 Insect Glycoprotein N-Glycan Structure 268
7.3.1 Typical N-Glycan Structures 268
7.3.2 Hybrid/Complex N-Glycans 270
7.3.3 Sialylated N-Glycans 270
7.3.4 Summary 270
7.4 N-Glycan Processing Enzymes in the BEVS 272
7.4.1 Processing P-N-Acetylglucosaminidase 272
7.4.2 Core al,3 Fucosyltransferase 272
7.4.3 Lack of Mannose-6-Phosphate 272
7.5 Lack of Glycosyltransferases 273
7.5.1 N-Acetylglucosaminyltransferases II—IV 273
7.5.2 N-acetylgalactosaminyl-Galactosyl-and Sialyltransferase 273
7.5.3 Glycosyltransferase Donor Substrates 274
7.6 Useof Baculoviruses to Extend BEVS N-Glycosylation 274
7.6.1 Promoter Choice 274
7.6.2 Baculovirus Encoded Glycosyltransferases 275
X Contents
7.6.2.1 N-Acetylglucosaminyltransferase I 175
7.6.2.2 Galactosyltransferase 175
7.6.2.3 Sialyltransferase 175
7.6.2.4 N-acetylglucosaminyltransferase II 176
7.6.2.5 Trans-Sialidase 176
7.6.3 Baculoviruses Encoded Sugar Processing Genes 176
7.6.3.1 UDP-GlcNAc 2-Epimerase/N-Acetylmannosamine Kinase 176
7.6.3.2 Sialic Acid Synthetase 177
7.6.3.3 CMP-Sialic Acid Synthetase 177
7.6.4 Summary 177
7.7 Transgenic Insect Cell lines 178
7.7.1 Proof of Concept 178
7.7.2 Transgenic Glycosyltransferases 179
7.7.2.1 Galactosyltransferase 179
7.7.2.2 Sialyltransferase 179
7.7.2.3 N-Acetylglucosaminyltransferase II 180
7.7.3 Transgenic Sugar Processing Genes 180
7.7'.4 Use of Transposon-Based Systems 181
7.7.5 Summary 181
7.8 Sugar Supplementation 182
7.9 Future Directions 182
7.9.1 Completing the N-Glycosylation Pathway 183
7.9.2 Reducing Deleterious Activities 183
References 184
8 Getting Bacteria to Clycosylate 193
Michael Kowarik and Mario F. Feldman
8.1 Introduction 193
8.1.1 Overview and Background 193
8.1.2 Bacterial Protein Glycosylation 194
8.2 N-Glycosylation 194
8.2.1 Introduction 194
8.2.2 The Acceptor Protein 195
8.2.2.1 Primary Acceptor Consensus 196
8.2.2.2 Conformational Requirements for N-Glycosylation 196
8.2.2.3 Crystal Structures of Bacterial N-Glycoproteins 197
8.2.3 The LLO Substrate and the N-OTase, PglB 197
8.3 O-Glycosylation 199
8.3.1 O-Glycosylation in Pseudomonas aeruginosa 200
8.3.1.1 Introduction 200
8.3.1.2 The Acceptor Protein for O-Glycosylation 200
8.3.1.3 Glycan Structures in P. aeruginosa O-Glycosylation 201
8.3.2 O-Glycosylation in Neisseria 201
8.3.2.1 Introduction 201
8.3.2.2 PglL, the O-OTase of N. meningitidis 201
Contents XI
8.3.2.3 Glycan Substrates for N. meningitidis O-Glycosylation 202
8.4 Exploitation of N- and O-Iinked Glycosylation 203
8.4.1 Therapeutic (Human) Proteins 203
8.4.2 Bioconjugate Vaccines 204
8.4.3 Glycoengineering 205
References 206
Part Two Other Modifications 209
9 Biopharmaceuticals: Post-Translational Modification Carboxylation
and Hydroxylation 211
Mark A. Brown and Leisa M. Stenberg
9.1 Introduction 211
9.2 Y-Carboxylation 211
9.2.1 Biological Function of y-Carboxylation 211
9.2.2 The Gla Domain 214
9.2.3 Biosynthesis of Gla 217
9.2.4 y-Carboxylated Biopharmaceuticals 219
9.2.4.1 Factor IX 219
9.2.4.2 Factor Vila 221
9.2.4.3 Protein C/Activated Protein C 222
9.2.4.4 Prothrombin 223
9.2.4.5 Conotoxins 224
9.2.5 Enhancement of Cellular Carboxylation Capacity 224
9.2.5.1 Enhanced Expression of the y-Carboxylation Machinery 225
9.2.5.2 Inhibition of Calumenin Expression 226
9.2.5.3 Propeptide/Propeptidase Engineering 226
9.2.6 Purification of y-Carboxylated Proteins 226
9.2.7 Analytical Characterization of y-Carboxylated Proteins 227
9.2.7.1 Methods for Detecting Gla 227
9.2.7.2 Metal Content 227
9.2.7.3 Metal Binding-Induced Structural Changes 228
9.2.7.4 Phospholipid Membrane Binding Assays 228
9.2.7.5 y-Carboxylase Enzyme Assays 228
9.3 Post-Translational Hydroxylation 229
9.3.1 Biological Function of Hydroxylation 229
9.3.2 Biosynthesis of Hydroxylated Amino Acids 231
9.3.2.1 Biosynthesis of Hya/Hyn 231
'i.'i.l.l Biosynthesis of Hydroxyproline 232
9.3.3 Hydroxylated Biopharmaceuticals 233
9.3.3.1 Factor IX 233
9.3.3.2 Protein C/Activated Protein C 233
9.3.3.3 Conotoxins 234
9.3.4 Analytical Characterization of P-Hydroxylated Proteins 235
9.3.4.1 Methods for Detecting Hya/Hyn 235
XII Contents
9.3.4.2 P-Hydroxylase Enzyme Assays 235
9.4 Conclusions 235
References 236
10 C-Terminal a-Amidation 253
Nozer M. Mehta, Sarah E. Carpenter, and Angelo P. Consalvo
10.1 Introduction 253
10.2 Substrate Specificity of PAM 253
10.3 Activity of PAM 254
10.3.1 Assays for Measurement of PAM Activity 254
10.3.2 Mechanism of Action 255
10.3.3 Species Distribution of a-Amidated Peptides and PAM 257
10.4 Genomic Structure and Processing of PAM 257
10.4.1 Organization of the PAM Gene 257
10.4.2 Tissue-Specific Forms of PAM 258
10.5 Structure-Activity Relationships (SAR) for Rat PAM Activity 258
10.6 a-Amidation of Glycine-Extended Peptides 260
10.6.1 In Vitro a-Amidation 260
10.6.2 Optimization of the PAM Reaction In Vitro 261
10.7 Cloning and Expression of Various Forms of PAM 263
10.7.1 PHM, PHMcc and PAL 264
10.7.2 Bifunctional PAM 264
10.7.3 Co-expression of PAM with Glycine-Extended Peptides 265
10.8 A Process for Recombinant Production of a-Amidated Peptides 265
10.8.1 Expression of Glycine-Extended Peptides in E. coli by a Direct Expression
Process 266
10.8.2 Purification of the Glycine-Extended Peptides 266
10.8.3 Expression of PAM in CHO Cells 267
10.8.4 Purification of Recombinant PAM (rPAM) 267
10.8.5 Post-Amidation Purification 268
10.8.6 Expression Levels of Peptides by Direct Expression Technology 269
10.9 Marketed Peptides 269
10.9.1 Marketed a-Amidated Peptides 269
10.10 Conclusions 271
References 271
11 Disulfide Bond Formation 277
Hayat El Hajjaji andJean-Frangois Collet
11.1 Introduction 277
11.2 Disulfide Bonds have a Stabilizing Effect 278
11.3 Disulfide Bond Formation is a Catalyzed Process 278
11.4 Disulfide Bond Formation in the Bacterial Periplasm 278
11.4.1 The Oxidation Pathway: DsbA and DsbB 279
11.4.1.1 DsbA, a very Oxidizing Protein 279
11.4.1.2 DsbB 280
Contents XIII
11.4.1.3 DsbB is Reoxidized by the Electron Transport Chain 280
11.4.1.4 Engineering of a New Oxidation Pathway 281
11.4.2 Disulfide Isomerization Pathway 282
11.4.2.1 DsbC, a Periplasmic Protein Disulfide Isomerase 282
11.4.2.2 DsbC is a Dimeric Protein 284
11.4.2.3 DsbC is Kept Reduced by DsbD 284
11.4.2.4 DsbC can Function Independently of DsbD 285
11.4.2.5 DsbG, a Controversial Protein Disulfide Isomerase 285
11.5 Disulfide Bond Formation in the Cytoplasm 286
11.6 Formation of Protein Disulfide Bond in Heterologous Proteins
Expressed in E. coli 288
11.7 Disulfide Bond Formation in the Endoplasmic Reticulum 288
11.7.1 PDI Functions both as an Oxidase and an Isomerase 288
11.7.2 PDI is Reoxidized by Erol 289
11.7.3 Regulation of Erol 290
11.8 Conclusions 290
References 290
Part Three Engineering of PTMS 295
12 Glycoengineering of Erythropoietin 297
Steve Elliott
12.1 Introduction 297
12.2 Endogenous Epo, rHuEpo and their Attached Carbohydrates 298
12.2.1 Rules for Attachment of Carbohydrates 300
12.2.2 Carbohydrate Glycoforms and their Effect on Structure and
Activity 302
12.2.3 Glycoengineering of New Molecules - Darbepoetin Alfa 303
12.2 A Glycoengineering of New Molecules - AMG114 307
12.2.5 Glycoengineered ESAs and Biological Activity 308
12.3 Effect of Carbohydrate on Clearance, Mechanism of Clearance 309
References 311
13 Glycoengineering: Cerezyme as a Case Study 319
Scott M. Van Patten and Tim Edmunds
13.1 Introduction 319
13.2 Basis for Glycan-Directed Enzyme Replacement Therapy
forLSDs 319
13.2.1 Lysosomal Storage Diseases 319
13.2.2 Gaucher Disease 320
13.2.3 Glucocerebrosidase 321
13.2.4 Enzyme Replacement as a Therapy for LSDs 322
13.3 Use of Placental Glucocerebrosidase for ERT 323
13.3.1 Initial Clinical Studies with Unmodified GCase Isolated from
Placenta 323
XIV Contents
13.3.2 Identification of Mannose Receptor and its Role in
Macrophage Uptake 324
13.3.3 Glycoengineering via Sequential Removal of Glycans 324
13.3.4 Development of First ERT for Gaudier Disease - Ceredase 325
13.4 Development of a Second-Generation ERT using Recombinant
Technology 327
13.4.1 Production of a CHO Cell-Expressed Recombinant Human
GCase - Cerezyme 327
13.4.2 Biochemical Comparison of Cerezyme to Ceredase 327
13.4.3 Comparison of Ceredase to Cerezyme In Vivo 329
13.5 Alternative Strategies for Glycoengineered GCase 330
13.5.1 Overview of Possible Strategies for Targeting Mannose Receptor 330
13.5.2 Use of Mannosidase Inhibitors 330
13.5.3 Use of Mutant Cell lines 333
USA Use of Alternative Expression Systems 333
13.6 Summary 334
References 334
14 Engineering in a PTM: PECylation 341
Cian Maria Bonora and Francesco Maria Veronese
14.1 Protein PEGylation 341
14.2 General Properties of PEG 343
14.3 Chemically Activated PEGs and the Process of PEGylation 344
14 A Potential Effects of PEGylation that are of Therapeutic Relevance 347
14.5 Some Specific PEGylated Biopharmaceuticals 349
14.6 Conclusions 352
References 353
Index 359 |
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| discipline | Chemie / Pharmazie Biologie Chemie Medizin |
| format | Book |
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| genre | (DE-588)4143413-4 Aufsatzsammlung gnd-content |
| genre_facet | Aufsatzsammlung |
| id | DE-604.BV035799567 |
| illustrated | Illustrated |
| indexdate | 2024-07-20T10:22:33Z |
| institution | BVB |
| isbn | 9783527320745 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-018658728 |
| oclc_num | 302080461 |
| open_access_boolean | |
| owner | DE-20 DE-19 DE-BY-UBM DE-91G DE-BY-TUM DE-11 DE-B768 DE-M49 DE-BY-TUM |
| owner_facet | DE-20 DE-19 DE-BY-UBM DE-91G DE-BY-TUM DE-11 DE-B768 DE-M49 DE-BY-TUM |
| physical | XIX, 370 S. Ill., graph. Darst. |
| publishDate | 2009 |
| publishDateSearch | 2009 |
| publishDateSort | 2009 |
| publisher | Wiley-VCH |
| record_format | marc |
| spelling | Post-translational modification of protein biopharmaceuticals ed. by Gary Walsh Weinheim Wiley-VCH 2009 XIX, 370 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Biopharmaceutics methods Biotechnology methods Glycosylation Pharmaceutical biotechnology Post-translational modification Protein Engineering methods Protein Processing, Post-Translational Proteins analysis Posttranslationale Änderung (DE-588)4204069-3 gnd rswk-swf Proteinpräparat (DE-588)4247384-6 gnd rswk-swf Rekombinantes Protein (DE-588)4277353-2 gnd rswk-swf Biopharmazie (DE-588)4006890-0 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content Proteinpräparat (DE-588)4247384-6 s Rekombinantes Protein (DE-588)4277353-2 s Posttranslationale Änderung (DE-588)4204069-3 s Biopharmazie (DE-588)4006890-0 s DE-604 Walsh, Gary Sonstige (DE-588)13591714X oth text/html http://deposit.dnb.de/cgi-bin/dokserv?id=3192076&prov=M&dok_var=1&dok_ext=htm Inhaltstext HBZ Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=018658728&sequence=000004&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Post-translational modification of protein biopharmaceuticals Biopharmaceutics methods Biotechnology methods Glycosylation Pharmaceutical biotechnology Post-translational modification Protein Engineering methods Protein Processing, Post-Translational Proteins analysis Posttranslationale Änderung (DE-588)4204069-3 gnd Proteinpräparat (DE-588)4247384-6 gnd Rekombinantes Protein (DE-588)4277353-2 gnd Biopharmazie (DE-588)4006890-0 gnd |
| subject_GND | (DE-588)4204069-3 (DE-588)4247384-6 (DE-588)4277353-2 (DE-588)4006890-0 (DE-588)4143413-4 |
| title | Post-translational modification of protein biopharmaceuticals |
| title_auth | Post-translational modification of protein biopharmaceuticals |
| title_exact_search | Post-translational modification of protein biopharmaceuticals |
| title_full | Post-translational modification of protein biopharmaceuticals ed. by Gary Walsh |
| title_fullStr | Post-translational modification of protein biopharmaceuticals ed. by Gary Walsh |
| title_full_unstemmed | Post-translational modification of protein biopharmaceuticals ed. by Gary Walsh |
| title_short | Post-translational modification of protein biopharmaceuticals |
| title_sort | post translational modification of protein biopharmaceuticals |
| topic | Biopharmaceutics methods Biotechnology methods Glycosylation Pharmaceutical biotechnology Post-translational modification Protein Engineering methods Protein Processing, Post-Translational Proteins analysis Posttranslationale Änderung (DE-588)4204069-3 gnd Proteinpräparat (DE-588)4247384-6 gnd Rekombinantes Protein (DE-588)4277353-2 gnd Biopharmazie (DE-588)4006890-0 gnd |
| topic_facet | Biopharmaceutics methods Biotechnology methods Glycosylation Pharmaceutical biotechnology Post-translational modification Protein Engineering methods Protein Processing, Post-Translational Proteins analysis Posttranslationale Änderung Proteinpräparat Rekombinantes Protein Biopharmazie Aufsatzsammlung |
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| work_keys_str_mv | AT walshgary posttranslationalmodificationofproteinbiopharmaceuticals |