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Summary
Summary
This volume reviews the unlimited possibilities that appear to be opening up as a result of developments in glycotechnology and the physiological significance of endoglycosidases leading to new avenues in the field. Endoglycosidases are one of the general types of glycosidases and hydrolyze internal glycosidic bonds of oligosaccharide and polysaccharide chains, resulting in the release not of monosaccharides, but oligosaccharides. On the other hand, exoglycosidases (which act on nonreducing end sites of carbohydrate chains and as a result release a monosaccharide) corresponding to al most all of the glycosidic bonds of the known carbohydrate chains of glycocon- gates have been discovered. Some endoglycosidases, for example, amylase, cellulase and hyaluronidase, were previously known. However, except for hyaluronidase, the endoglycosidases which act on a long carbohydrate chain of glycoconjugates (glycoproteins, gly- lipids and proteoglycans) have not been investigated. The original enzymes for the inborn error of metabolism on the carbohydrate chains of glycoconjugates are exoglycosidases and related enzymes on the degra dation processes of carbohydrate chains, and the mechanism of glycoconjugate metabolism is explained by the exoglycosidases. Therefore, there was little or no awareness of the many kinds of endoglycosidases that exist. In order to elucidate the degradation mechanism of glycoconjugates, the uri nary carbohydrates were examined, resulting in the identification of many kinds of oligosaccharides and polysaccharides which are free from amino acids and pep tides. Thus it was suggested that many kinds of endoglycosidases which act on in ternal sites of carbohydrate chains exist in the animal body."
Table of Contents
| List of Contributors | p. v |
| Preface | p. vii |
| 1 Biochemistry of Glycoconjugates | p. 1 |
| 1.1 Chemical Structures | p. 1 |
| 1.1.1 Structures and Basic Properties of Carbohydrates | p. 1 |
| 1.1.2 Structures of Glycoproteins | p. 8 |
| 1.1.3 Structures of Proteoglycans and Glycosaminoglycans | p. 11 |
| 1.1.4 Structures of Glycolipids | p. 15 |
| 1.2 Enzyme Activity | p. 19 |
| 1.2.1 Measurement of the Amount of Protein | p. 19 |
| 1.2.2 Measurement of Initial Reaction Velocity | p. 21 |
| 1.2.3 Kinetics of Enzyme Activity | p. 23 |
| 1.2.4 Other Factors Influencing Enzyme Activity | p. 26 |
| 1.3 Purification of Enzymes | p. 26 |
| 1.3.1 Homogenation and Disruption of Cells and Tissues | p. 27 |
| 1.3.2 Salting Out and Dialysis | p. 28 |
| 1.3.3 Gel Filtration | p. 31 |
| 1.3.4 Ion-exchange Chromatography | p. 33 |
| 1.3.5 Affinity Chromatography | p. 37 |
| 1.3.6 Other Chromatographic Techniques | p. 39 |
| 1.3.7 Gel Electrophoresis | p. 42 |
| 1.4 Cloning of Endoglycosidases | p. 44 |
| 1.4.1 Peptide Purification and Determination of a Partial Amino Acid Sequence of Endo-A | p. 46 |
| 1.4.2 Polymerase Chain Reaction and Primer Selection | p. 47 |
| 1.4.3 Molecular Cloning and Sequence Analysis of the Endo-A Gene | p. 48 |
| 1.4.4 Gene Probes from Conserved Sequences of Endo-[Beta]-N-acetylglucosaminidases | p. 49 |
| 1.4.5 Expression and Purification of Endo-A from Escherichia coli | p. 49 |
| 1.4.6 Random Mutagenesis of the Endo-A Gene | p. 50 |
| References | p. 51 |
| 2 General Introduction of Various Endoglycosidases | p. 55 |
| 2.1 Endoglycosidases That Relate to N-Glycans | p. 55 |
| 2.1.1 Endo-[Beta]-N-acetylglucosaminidase | p. 55 |
| 2.1.2 Endo-[Beta]-mannosidase | p. 74 |
| 2.2 Endoglycosidases That Relate to O-Glycans | p. 84 |
| 2.2.1 Endo-[Alpha]-N-acetylgalactosaminidases | p. 84 |
| 2.2.2 An Unusual GlcNAc[Alpha]1-4Gal-releasing Endo-[Beta]-galactosidase | p. 94 |
| 2.3 Endoglycosidases That Relate to Proteoglycans | p. 101 |
| 2.3.1 Endo-[Beta]-xylosidase | p. 103 |
| 2.3.2 Endo-[Beta]-galactosidase | p. 105 |
| 2.3.3 Endo-[Beta]-glucuronidase | p. 107 |
| 2.4 Endoglycosidases That Relate to Glycosphingolipids | p. 110 |
| 2.4.1 Endoglycoceramidase | p. 110 |
| 2.4.2 Endo-[Beta]-galactosidase | p. 118 |
| References | p. 121 |
| 3 Enzymatic Synthesis of Neo-N-glycans | p. 129 |
| 3.1 Chemo-enzymatic Synthesis of Neoglycoconjugates Using Endo-[Beta]-N-acetylgIucosaminidase | p. 129 |
| 3.1.1 General Method for Chemo-enzymatic Synthesis of Glycopeptide | p. 129 |
| 3.1.2 Chemo-enzymatic Synthesis of Bioactive Glycopeptide Using Endoglycosidase | p. 140 |
| 3.1.3 Enzymatic Synthesis of Neoglycoconjugates Using Oligosaccharide-transfer Activity of Endo-A | p. 149 |
| 3.2 Remodeling of Sugar Chains in Glycoproteins Using Endo-[Beta]-N-acetylglucosaminidase | p. 154 |
| 3.2.1 Remodeling of Sugar Chains by Endo-A | p. 154 |
| 3.2.2 Remodeling of Sugar Chains by Endo-M | p. 159 |
| 3.3 Synthesis of [Beta]-Mannosides Using Endo-[Beta]-mannosidase | p. 162 |
| 3.3.1 Synthesis of the Man[Beta]1-4GlcNAc Structure | p. 162 |
| 3.3.2 Discovery of Transglycosylation Activity of Endo-[Beta]-mannosidase | p. 163 |
| 3.3.3 Transfer of Mannose to GlcNAc by [Beta]1-4 Linkage Using Endo-[Beta]-mannosidase | p. 165 |
| 3.3.4 Transfer of Oligomannose to GN2 Using Endo-[Beta]-mannosidase | p. 165 |
| 3.3.5 Transfer of Mannose to Various Monosaccharides Using Endo-[Beta]-mannosidase | p. 167 |
| 3.3.6 Future Prospects | p. 168 |
| References | p. 168 |
| 4 Enzymatic Synthesis of Neo-O-glycans | p. 173 |
| 4.1 Enzymatic Synthesis of O-Linked Glycopeptides Using Endo-[Alpha]-N-acetylgalactosaminidase | p. 173 |
| 4.1.1 One-step Synthesis of O-Linked Glycopeptides Using Endo-[Alpha]-GalNAc-ase | p. 174 |
| 4.1.2 Transglycosylation Using Endo-[Alpha]-GalNAc-ase from Streptococcus pneumoniae | p. 174 |
| 4.1.3 Transglycosylation Using Endo-[Alpha]-GalNAc-ase from Bacillus sp. | p. 175 |
| 4.1.4 Transglycosylation Using Endo-[Alpha]-GalNAc-ase from Streptomyces sp. | p. 175 |
| References | p. 178 |
| 5 Enzymatic Synthesis of Neoproteoglycans | p. 181 |
| 5.1 Enzymatic Synthesis of Neoglycans Using Hyaluronidase | p. 182 |
| 5.1.1 Hydrolysis Reaction of Hyaluronidase | p. 182 |
| 5.1.2 Transglycosylation with Hyaluronidase as an Endoglycosidase | p. 183 |
| 5.1.3 Reconstruction of GAG Chains Using Hyaluronidase | p. 189 |
| 5.1.4 GAG Library | p. 191 |
| 5.1.5 Construction of Neoglycan Attached to Core Protein by Transglycosylation with Hyaluronidase | p. 191 |
| 5.2 Enzymatic Synthesis of Neoproteoglycans Using Endo-[Beta]-xylosidase | p. 194 |
| 5.2.1 Introduction of GAG Chains into Peptide by Endo-[Beta]-xylosidase | p. 194 |
| 5.2.2 Cellulase That Plays an Alternative Role as Endo-[Beta]-xylosidase | p. 196 |
| References | p. 196 |
| 6 Enzymatic Synthesis of Neoglycolipids | p. 199 |
| 6.1 Enzymatic Synthesis of Neoglycolipids and Glycosphingolipids Derivatives Using Jellyfish Endoglycoceramidase | p. 199 |
| 6.1.1 Transfer of an Intact GM1a-oligosaccharide from GM1a to Various 1-Alkanols | p. 199 |
| 6.1.2 Synthesis of Fluorescence-labeled Glycosphingolipids | p. 202 |
| 6.1.3 Condensation Reaction | p. 203 |
| 6.1.4 Comparison with EGCases (Ceramide Glycanases) from Other Sources | p. 203 |
| References | p. 206 |
| 7 Analysis of Sugar Structures Using Endoglycosidase | p. 207 |
| 7.1 Analysis of Sugar Chain Structures Using Endo-[Beta]-N-acetylglucosaminidase | p. 207 |
| 7.1.1 Analysis of Asparagine-linked Sugar Chains of Gycoproteins | p. 207 |
| 7.1.2 Typing of Asparagined-linked Sugar Chains of Glycoproteins | p. 209 |
| 7.1.3 Specific Release of Complex Type Sugar Chains from Glycoproteins by Endo-HS | p. 210 |
| 7.2 Analysis of Sugar Chain Structures Using Endo-[Alpha]-N-acetyl-galactosaminidase | p. 218 |
| 7.2.1 Release of O-Linked Sugar Chain from Glycoprotein | p. 218 |
| 7.2.2 Release of O-Linked Sugar Chain from Asialofetuin Using Endo-[Alpha]-GalNAc-ase | p. 219 |
| 7.2.3 Release of O-linked Sugar Chain from Fetuin Using Endo-[Alpha]-GalNAc-ase | p. 220 |
| 7.3 Analysis of Sugar Chain Structures Using Endo-[Beta]-xylosidase Activity of Cellulase | p. 224 |
| 7.4 Analysis of Sugar Chain Structures Using an Endoglycoceramidase | p. 227 |
| 7.4.1 Isolation of GSLs from Biological Samples Using a Phenyl Boronate-conjugated Matrix Column | p. 228 |
| 7.4.2 Enzymatic Release of GSL-oIigosaccharides by EGCase and Their Purification | p. 230 |
| 7.4.3 Thin-layer Chromatography (TLC) of GSL-oligosaccharides and Immunostaining | p. 231 |
| 7.4.4 Anion-exchange HPLC of GSL-oligosaccharides with a Strong Alkaline Solvent System | p. 232 |
| 7.4.5 HPLC Separation of GSL-oligosaccharides Labeled with UV-absorptive or Fluorescent Probes and Two-dimensional HPLC Mapping | p. 232 |
| References | p. 236 |
| Appendix | p. 239 |
| List of Abbreviations | p. 247 |
| Index | p. 249 |
