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  • 1
    Online Resource
    Online Resource
    Newark :John Wiley & Sons, Incorporated,
    Keywords: Proteins-Biotechnology. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (315 pages)
    Edition: 1st ed.
    ISBN: 9781119053347
    Language: English
    Note: Cover -- Title Page -- Copyright -- Contents -- Preface -- About the Author -- Abbreviations -- Chapter 1 Introduction to Co‐ and Post‐translational Modifications of Proteins -- Brief Introductions to Individual Chapters -- Chapter 2: Acetylation of Proteins -- Chapter 3: C‐Terminal Lys or Arg Clipping of Proteins -- Chapter 4: Cysteinylation of Proteins -- Chapter 5: Deamidation of Proteins -- Chapter 6: Glycation of Proteins -- Chapter 7: Glycosylation of Proteins -- Chapter 8: N‐glycosylation of Proteins -- Chapter 9: O‐glycosylation of Proteins -- Chapter 10: Hydroxylation of Proteins -- Chapter 11: Methylation of Proteins -- Chapter 12: Oxidation of Proteins -- Chapter 13: Phosphorylation of Proteins -- Chapter 14: Prenylation of Proteins -- Chapter 15: Proteolysis of Proteins -- Chapter 16: Selenylation of Proteins -- Chapter 17: Signal Peptides of Proteins -- Chapter 18: Sulfation of Proteins and Glycoproteins -- Chapter 19: SUMOylation -- Chapter 20: Ubiquitination -- Chapter 21: Other PTMs -- References -- Chapter 2 Acetylation of Proteins -- Introduction -- Mechanism of N‐acetylation at the N‐termini of Proteins -- Mechanism of N‐acetylation and N‐deacetylation of Lysine Residues -- Mechanism of O‐acetylation of Sugar Residues -- Biological Significance of Protein Acetylation -- Acetylation in Recombinant Therapeutic Proteins -- Methods to Analyze Acetylation in Proteins and Carbohydrates -- References -- Chapter 3 C‐terminal Lys or Arg Clipping in Proteins -- Introduction -- Biological Significance of C‐terminal Lys or Arg Clipping in Proteins -- Analysis of C‐terminal Lys or Arg Clipping in Proteins -- References -- Chapter 4 Cysteinylation of Proteins -- Introduction -- Biological Significance of Cysteinylation of Proteins -- Cysteinylation and Trisulfide Bonds in Recombinant Therapeutic Proteins. , Analysis of Cysteinylation of Proteins -- References -- Chapter 5 Deamidation of Proteins -- Introduction -- Mechanism of Deamidation of Proteins -- Physicochemical Characteristics of Deamidated Proteins -- Biological Significance of Deamidation of Proteins -- Deamidation and Immunogenicity -- Deamidation and Pharmacokinetics Properties of Proteins -- Deamidation in Recombinant Therapeutic Proteins -- Methods for the Analysis of Deamidation in Proteins -- References -- Chapter 6 Glycation of Proteins -- Introduction -- Mechanism of Protein Glycation -- Glycation of Proteins in Human -- Protein Glycation and Human Diseases -- Glycation in Recombinant Therapeutic Proteins -- Methods to Analyze Protein Glycation -- References -- Chapter 7 Glycosylation of Proteins -- Introduction -- Glycans and Aglycans -- Glycosidic Bonds -- Aldoses and Ketoses -- Anomeric Groups: ‐ and ‐Configurations -- Natural Diversity of Glycans -- Glycans and Enzymes -- N‐glycosylation -- O‐glycosylation -- Phospho‐Serine Glycosylation -- GPI‐Anchors (Glypiation) -- C‐mannosylation -- References -- Chapter 8 N‐glycosylation of Proteins -- Introduction -- Mechanism of N‐glycosylation of Proteins -- Biosynthesis of N‐Glycans -- Biosynthesis of Lipid‐linked Precursor Oligosaccharide -- En Bloc Transfer of the Precursor Oligosaccharide to Nascent Polypeptide Chain -- Processing of the Glycan -- Additional Processing of Oligosaccharide Unit for Chain Elongation and/or Modifications -- Microheterogeneity of N‐Glycans -- Species‐Specific N‐glycosylation -- Functions of N‐glycans -- Physicochemical Functions of N‐glycans -- Biological Functions of N‐glycans -- Impact of N‐Glycans on Pharmacokinetic Properties of Proteins -- N‐Glycans and Human Diseases -- N‐glycosylation of RTPs -- Methods to Analyze N‐Glycans -- References -- Chapter 9 O‐glycosylation of Proteins -- Introduction. , Biosynthesis of O‐Glycans -- Biosynthesis of Mucin Type O‐Glycans -- Biosynthesis of O‐linked GlcNAc on Proteins -- Biosynthesis of O‐linked Fucose on Proteins -- Biosynthesis of O‐linked Glc Residues -- Biosynthesis of O‐linked Gal Residues -- Biosynthesis of O‐linked Man Residues -- O‐Glycans on Hydroxyproline Residues -- Physicochemical Properties of O‐Glycosylated Proteins -- Biological Functions of O‐Glycans -- O‐glycosylation in RTPs -- Analysis of O‐Glycans -- References -- Chapter 10 Hydroxylation of Proteins -- Introduction -- Mechanism of Hydroxylation -- Mechanism of Hydroxylation in Organic Molecules -- Mechanism of Hydroxylation in Biomolecules -- Prolyl 4‐Hydroxylase -- Prolyl 3‐Hydroxylase -- Lysyl 5‐Hydroxylase -- Phenylalanine Hydroxylase -- Tyrosine Hydroxylase -- Biological Significance of Hydroxylation -- Hydroxylation in RTPs -- Analysis of Hydroxylation -- References -- Chapter 11 Methylation of Proteins -- Introduction -- Mechanism of Protein Methylation -- Chemical Methylation Reactions -- Biological Methylation Reactions -- Methylation of Arg Residues -- Methylation of Lys Residues -- Methylation of Prenylcysteine Residues -- Methylation of Protein Phosphatase 2A -- Methylation of Isoaspartyl Residues -- O‐Methylation of Sugar Residues -- Physicochemical and Biological Significance of Methylation of Proteins -- Methylation in RTPs -- Methods to Analyze Methylation in Proteins and Glycoproteins -- References -- Chapter 12 Oxidation of Proteins -- Introduction -- Mechanism of Protein Oxidation -- Methionine (Met) Oxidation -- Cysteine (Cys) Oxidation -- Tryptophan (Trp) Oxidation -- Tyrosine (Tyr) Oxidation -- Oxidation of Other Amino Acid Residues and Protein Backbone -- Oxidation in RTPs -- Met Oxidation in mAbs -- Analytical Methods to Measure Protein Oxidation -- References -- Chapter 13 Phosphorylation of Proteins. , Introduction -- Mechanism of Protein Phosphorylation in Living Cells -- Mg2+ Mediated Mechanism of Protein Phosphorylation -- Protein Kinase‐Based Mechanism of Protein Phosphorylation -- Mechanism of Dephosphorylation of Proteins by Phosphatases -- Protein Kinases -- Serine Kinases -- Tyrosine Kinases -- Physicochemical and Biological Functions of Protein Phosphorylation -- Phosphorylation in RTPs -- Methods to Analyze Protein Phosphorylation -- Gel Electrophoresis -- Mass Spectrometry -- Enrichment of Phosphoproteins -- Enrichment of Phosphorylated Peptides -- References -- Chapter 14 Prenylation of Proteins -- Introduction -- Mechanism of Protein Prenylation -- Biological Significance of Prenylation of Proteins -- Analysis of Prenylation of Proteins -- References -- Chapter 15 Proteolysis of Proteins -- Introduction -- Chemical Proteolysis -- Enzymatic Proteolysis -- Biological Significance of Proteolysis -- Post‐translational Processing of Proteins by Proteolysis -- Intracellular and Extracellular Degradation of Proteins by Proteases -- Proteolysis and Food Digestion -- Role of Proteases in Apoptosis -- Role of Proteolysis in Human Diseases -- Use of Proteases in Laboratories -- Sources of Proteases -- Proteolysis in RTPs -- Chemical Proteolysis in RTPs -- Enzymatic Proteolysis in RTPs -- Analytical Methods for the Detection of Proteolysis of Proteins -- References -- Chapter 16 Selenylation -- Introduction -- Biological Significance of Selenylation of Proteins -- References -- Chapter 17 Signal Peptides -- Introduction -- Biological Significance of Signal Peptides -- Signal Peptides in RTPs -- References -- Chapter 18 Sulfation of Proteins and Glycoproteins -- Introduction -- Biosynthesis of PAPS -- Sulfation Reactions in the Cytosol -- Sulfation in the Golgi Compartments -- Sulfation of Tyrosine Residues -- Mechanism of Tyrosine Sulfation. , Biological Functions of Tyr Sulfation -- Sulfation of Glycosaminoglycans (GAGs) and Proteoglycans -- Biological Functions of GAGs -- Sulfation in RTPs -- Analysis of Sulfation in Biomolecules -- Analysis of Tyr Sulfation -- Analysis of Sulfated Glycoconjugates -- Colorimetric Methods to Analyze Sulfated Glycoconjugates -- Electrophoretic Methods to Analyze Sulfated Glycoconjugates -- Chromatographic Methods to Analyze Sulfated Glycoconjugates -- Analysis of Sulfated Glycoconjugates by Mass Spectrometry -- References -- Chapter 19 SUMOylation -- Introduction -- Mechanism of SUMOylation -- Biological Significance of SUMOylation -- References -- Chapter 20 Ubiquitination -- Introduction -- Mechanism of Ubiquitination -- Biological Significance of Ubiquitination -- References -- Chapter 21 Other CTMs and PTMs of Proteins -- Adenylylation or AMPylation -- ADP‐Ribosylation -- Amidation -- Arginylation -- Butyrylation -- Carbamylation -- Carbonylation -- γ ‐Carboxylation -- Citrullination -- Diphthamide -- Formylation -- Glypiation -- Hypusine Formation -- Iodination -- Lipoylation -- Malonylation -- Myristoylation -- Neddylation -- Palmitoylation -- Polyglutamylation -- Polyglycylation -- Propionylation -- Pupylation -- Pyroglutamate Formation -- S‐Glutathionylation -- S‐Nitrosylation -- References -- Index -- Supplemental Images -- EULA.
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  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Carbohydrate Research 191 (1989), S. 333-341 
    ISSN: 0008-6215
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Carbohydrate Research 258 (1994), S. 243-254 
    ISSN: 0008-6215
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Carbohydrate Research 191 (1989), S. 321-332 
    ISSN: 0008-6215
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 0012-1606
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 0012-1606
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-0533
    Keywords: Key words Amyotrophic lateral sclerosis ; Neurofilament phosphorylation ; Primary neuronal cultures ; Cerebrospinal fluid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Amyotrophic lateral sclerosis (ALS), a neurodegenerative disease, is characterized by degeneration of lower and upper motor neurons. Serum and cerebrospinal fluid (CSF) of ALS patients have been found to exert toxic effects on neurons in culture. We report here increased phosphorylation of neurofilaments (NF) in the soma of chick spinal cord neurons in culture when exposed to CSF of ALS patients. Spinal cord neurons were cultured from 10-day embryonic chick and exposed to culture medium supplemented with CSF or serum (10   %) from ALS and non-ALS patients for 48 h. There was a significant increase in the number of neuronal soma staining with antibodies against phosphorylated NF, following exposure to CSF from ALS patients. Such an increase, however, was not observed in cultures exposed to serum from ALS patients and also serum and CSF from non-ALS patients. These results suggest that the CSF of ALS patients may contain factor(s) which induces aberrant phosphorylation of NF in the soma, a probable forerunner to the formation of neurofibrillary tangles and eventual degeneration of neurons.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1432-0533
    Keywords: Amyotrophic lateral sclerosis ; Neurofilament phosphorylation ; Primary neuronal cultures ; Cerebrospinal fluid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Amyotrophic lateral sclerosis (ALS), a neurodegenerative disease, is characterized by degeneration of lower and upper motor neurons. Serum and cerebrospinal fluid (CSF) of ALS patients have been found to exert toxic effects on neurons in culture. We report here increased phosphorylation of neurofilaments (NF) in the soma of chick spinal cord neurons in culture when exposed to CSF of ALS patients. Spinal cord neurons were cultured from 10-day embryonic chick and exposed to culture medium supplemented with CSF or serum (10%) from ALS and non-ALS patients for 48 h. There was a significant increase in the number of neuronal soma staining with antibodies against phosphorylated NF, following exposure to CSF from ALS patients. Such an increase, however, was not observed in cultures exposed to serum from ALS patients and also serum and CSF from non-ALS patients. These results suggest that the CSF of ALS patients may contain factor(s) which induces aberrant phosphorylation of NF in the soma, a probable forerunner to the formation of neurofibrillary tangles and eventual degeneration of neurons.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    European journal of pediatrics 147 (1988), S. 162-167 
    ISSN: 1432-1076
    Keywords: Bovine Surfactant TA ; Hyaline membrane disease ; Preterm baboons ; Mean airway pressure ; Pressure/volume curves
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The responses of Surfactant TA instillation in two groups of premature lambs (Group I, 124.8±1.1 days and Group II, 132.2±1.2 days, mean±SD) and one group of premature baboons (140±1.6 days) were compared to study the effectiveness of the same surfactant in different animal models. The treatment group received Surfactant TA 100 mg/kg surfactant lipid at 1 to 2 h of age. Control lambs and baboons did not receive surfactant. Sequential measurements of arterial blood gas tension, acid base status, mean airway pressure (MAP) and oxygen requirement (FiO2) were carried out for 8h after surfactant instillation. The results show that the Group I surfactant-treated lambs improved significantly following instillation. The a/APO2 improved from 0.08±0.02 before treatment to 0.31±0.12, and the MAP decreased from 15.8±0.9 cm H2O to 13.3±1.3 cm H2O 2.5 h after treatment. At 5.5 h after treatment, the lambs given surfactant deteriorated. Group II treated lambs showed sustained improvement throughout the study period, and improvement in the treated group was not significantly different from Group II control lambs. The surfactant-treated baboons, however showed sustained and significant improvement in a/APO2 from the time of instillation to the end of the study. These data suggest that the differences in response to the same surfactant therapy between the lamb and baboon models were due to related differences in species, lung maturation, and the differences in response to surfactant, i.e., alveolar leak of protein.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1573-4986
    Keywords: polysaccharide components ; pseudo-stem (scape) ; Musa paradisiaca ; carbohydrates ; structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Polysaccharide components present in the pseudo-stem (scape) of M. paradisiaca were purified from acetone powder of the scape by delignification followed by extraction with aqueous solvents into water soluble polysaccharide (WSP), EDTA-soluble polysaccharide (EDTA-SP), alkali-soluble polysaccharide (ASP) and alkali-insoluble polysaccharide (AISP) fractions. Sugar compositional analysis showed that WSP and EDTA-SP contained only D-Glc whereas ASP contained D-Glc, L-Ara and D-Xyl in ∼ 1:1:10 ratio, respectively, and AISP' contained D-Glc, L-Ara and D-Xyl in ∼ 10:1:2 ratio, respectively. WSP was further purified by complexation with iso-amylalcohol and characterized by specific rotation, IR spectroscopy, Iodine affinity, ferricyanide number, blue value, hydrolysis with α-amylase and glucoamylase, and methylation linkage analysis, and shown to be a amylopectin type α-D-glucan.
    Type of Medium: Electronic Resource
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