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6 Appendix Figure 30: GPC fractionation of mouse brain glycoproteins. The four protein-containing fractions of experiment (A) and (B) are depicted in silver-stained gels. The fraction F2 (underlined) was used for preparative SDS-PAGE. Figure 31: Protein fractions generated by preparative SDS-PAGE of mouse brain glycoproteins after GPC. Some of the protein-containing fractions of experiments (A) and (B) are depicted in silverstained gels. Western blots against neurofascin show the presence of NF186 in F19 (A) and F15 to F17 (B). 77
6 Appendix Figure 32: O-Glycan analysis of permethylated O-glycan alditols from mouse NCAM1. Dashed arrows indicate the loss of methyl and sodium (-36) and fragments of polysialic acid are indicated with a star. The monoisotopic signal at 1098.8 Da (see upper insert for MS/MS) corresponds to three neuraminic acid residues without a reduced end. The lower insert shows the Mascot results from the protein identification of this NCAM1 preparation. 78
Page 1 and 2:
Identification and Characterization
Page 3 and 4:
I Index I Index of Contents I INDEX
Page 5 and 6:
I Index FIGURE 13: WESTERN BLOT OF
Page 7 and 8:
I Index I.III List of Abbreviations
Page 9 and 10:
I Index PBS PMT PNN Phosphate Buffe
Page 11 and 12:
I Index I.III.II Amino acids - thre
Page 13 and 14:
I Index II Zusammenfassung Die O-Ma
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1 Introduction glycosidically linke
Page 17 and 18:
1 Introduction glycans, complex-typ
Page 19 and 20:
1 Introduction O-glycosylation (typ
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1 Introduction Figure 3: Schematic
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1 Introduction the sites and functi
Page 25 and 26:
1 Introduction posttranslational pr
Page 27 and 28:
1 Introduction transfer of mannose
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1 Introduction Together the above m
Page 31 and 32:
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
Page 39 and 40: 2 Materials and methods (see 2.2.2.
Page 41 and 42: Figure 9: O-Glycome of mouse brain.
Page 43 and 44: 3 Results Table 1: Sequential extra
Page 45 and 46: 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: 6 Appendix Table 8: Protein identif
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 and 98: 6 Appendix Figure 40: Calf brain-de
Page 99 and 100: 6 Appendix Table 13: Protein identi
Page 101 and 102: 6 Appendix Table 14: Summary of hum
Page 103: Erklärung Ich versichere, dass ich
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