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6 Appendix Figure 41: Analysis of the MAG-containing fraction F14 from experiment (A). The MALDI-MS spectrum shows the permethylated glycan alditols. Arrows indicate signals derived by a loss of a methyl group and sodium (-36 Da). Signals marked by CS are a result of unspecific cleavage of chondroitin sulfate chains. The insert shows the results of protein identification in the respective fraction by ESI-MS/MS. 85
6 Appendix Table 13: Protein identification based on Mascot score of the lectican-containing fraction F11 from experiment (A). Protein (bovine) Score Serum albumin 996 Clusterin 709 Actin, cytoplasmic 1 401 Tubulin α-1B chain 217 Calmodulin 198 α-1-Acid glycoprotein 130 Apolipoprotein D 121 Neurocan core protein 102 Myelin basic protein 96 ATP synthase subunit δ, mitochondrial 93 CD99 antigen-like protein 2 92 Figure 42: Analysis of the lectican-containing fraction F11 from experiment (A). The MALDI-MS spectrum shows the permethylated glycan alditols. Monoisotopic masses corresponding to O-mannosyl glycans are underlined. Glycan fragments without a reduced end are indicated with an asterisk, arrows indicate signals derived by a loss of a methyl group and sodium (-36 Da). Signals marked by CS are a result of unspecific cleavage of chondroitin sulfate chains. 86
Page 1 and 2:
Identification and Characterization
Page 3 and 4:
I Index I Index of Contents I INDEX
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I Index FIGURE 13: WESTERN BLOT OF
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I Index I.III List of Abbreviations
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I Index PBS PMT PNN Phosphate Buffe
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I Index I.III.II Amino acids - thre
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I Index II Zusammenfassung Die O-Ma
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1 Introduction glycosidically linke
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1 Introduction glycans, complex-typ
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1 Introduction O-glycosylation (typ
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1 Introduction Figure 3: Schematic
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1 Introduction the sites and functi
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1 Introduction posttranslational pr
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1 Introduction transfer of mannose
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1 Introduction Together the above m
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1 Introduction 1.4 Aim of this proj
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2 Materials and methods Lysis and W
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2 Materials and methods 2.1.3.2 Sec
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2 Materials and methods 2.2.1.7 Fra
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2 Materials and methods (see 2.2.2.
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Figure 9: O-Glycome of mouse brain.
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3 Results Table 1: Sequential extra
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3 Results that this protein might b
Page 47 and 48: 3 Results 3.2 O-Mannosylation on ne
Page 49 and 50: 3 Results identified by several 361
Page 51 and 52: 3 Results Figure 15: Fragmentation
Page 53 and 54: 3 Results Table 2: Protein identifi
Page 55 and 56: 3 Results Three other O-mannosyl gl
Page 57 and 58: 3 Results 3.3 O-Mannosylation of le
Page 59 and 60: 3 Results 3.3.2 Recombinant express
Page 61 and 62: 3 Results identified just as the gl
Page 63 and 64: 3 Results Subsequentially, the resu
Page 65 and 66: 3 Results In order to get more info
Page 67 and 68: 3 Results brain-specific protein ne
Page 69 and 70: 4 Summary and outlook malformations
Page 71 and 72: 4 Summary and outlook O-mannosylati
Page 73 and 74: 4 Summary and outlook Figure 24: Sc
Page 75 and 76: 5 References Bleckmann, C., Geyer,
Page 77 and 78: 5 References Frischknecht, R. & Sei
Page 79 and 80: 5 References Kriebel, M., Metzger,
Page 81 and 82: 5 References Nizet, V. & Esko, J. (
Page 83 and 84: 5 References Susuki, K. & Rasband,
Page 85 and 86: 6 Appendix 6 Appendix Table 6: Summ
Page 87 and 88: 6 Appendix Figure 27: Comparison be
Page 89 and 90: 6 Appendix Table 8: Protein identif
Page 91 and 92: 6 Appendix Figure 32: O-Glycan anal
Page 93 and 94: 6 Appendix Figure 34: ESI-MS/MS of
Page 95 and 96: 6 Appendix Figure 38: Analysis of t
Page 97: 6 Appendix Figure 40: Calf brain-de
Page 101 and 102: 6 Appendix Table 14: Summary of hum
Page 103: Erklärung Ich versichere, dass ich
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