Structure and function of the plasma protein fetuin-B:
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| 035 | |a (OCoLC)1157261007 | ||
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| 100 | 1 | |a Schmitz, Carlo |e Verfasser |0 (DE-588)1200482824 |4 aut | |
| 245 | 1 | 0 | |a Structure and function of the plasma protein fetuin-B |c vorgelegt von M. Sc. Carlo Schmitz |
| 264 | 1 | |a Aachen |c [2019] | |
| 300 | |a 163 Seiten |b Illustrationen |c 21 cm | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
| 338 | |b nc |2 rdacarrier | ||
| 502 | |b Dissertation |c RWTH Aachen |d 2019 | ||
| 655 | 7 | |0 (DE-588)4113937-9 |a Hochschulschrift |2 gnd-content | |
| 856 | 4 | 2 | |m B:DE-101 |q application/pdf |u https://d-nb.info/1207483621/04 |3 Inhaltsverzeichnis |
| 856 | 4 | 2 | |m DNB Datenaustausch |q application/pdf |u http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=032280064&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |3 Inhaltsverzeichnis |
| 999 | |a oai:aleph.bib-bvb.de:BVB01-032280064 | ||
Datensatz im Suchindex
| _version_ | 1804181716557889536 |
|---|---|
| adam_text | TABLE
OF
CONTENTS
SUMMARY
..................................................................................................................................
6
ZUSAMMENFASSUNG
..............................................................................................................
8
I
INTRODUCTION
..................................................................................................................
10
1
T
HE
C
YSTATIN
S
UPERFAMILY
............................................................................................
10
1.1
CYSTATIN
STRUCTURE
AND
INHIBITORY
CHARACTERISTICS
......................................................
12
2
F
ETUIN
FAMILY
PROTEINS
..................................................................................................
15
2.
1
GLYCOSYLATION
.............................................................................................................
18
2.2
BIOLOGICAL
FUNCTION
....................................................................................................
21
2.2.1
BIOLOGICAL
FUNCTION
OF
FETUIN-B
IN
FERTILIZATION
......................................................
22
3
M
ETALLOPROTEINASES
.....................................................................................................
25
3.1
A
STANDARD
ORIENTATION
FOR
METALLOPROTEINASES
.........................................................
26
3.2
ASTACIN
PROTEINASE
FAMILY
.........................................................................................27
3.2.1
CRAYFISH
ASTACIN
..................................................................................................
28
3.2.2
OVASTACIN
.............................................................................................................
30
II
MATERIALS
AND
METHODS
..........................................................................................
34
1
M
ATERIALS
........................................................................................................................
34
1.1
CHEMICALS
..................................................................................................................
34
1.2
DEVICES
......................................................................................................................
34
1.3
COMPUTER
SOFTWARE
AND
DATABASES
..........................................................................
35
2
A
NIMAL
EXPERIMENTS
......................................................................................................
36
2.
1
FETUB
AND
ASTI
GENOTYPING
........................................................................................
36
2.2 GENERATION
OF
FETUB
7
,
ASTF
7
DOUBLE
DEFICIENT
MICE
.................................................38
2.3
ZONA
PELLUCIDA
DIGESTION
...........................................................................................38
3
C
ULTIVATION
AND
STORAGE
OF
E.
COU
CELLS
..................................................................
39
3.1
CULTURE
MEDIA
AND
ANTIBIOTICS
...................................................................................
39
3.2
SUSPENSION
AND
PLATE
CULTURES
.................................................................................
39
3.3
STORAGE
OF
E.
COLI
CELLS
..............................................................................................40
4
M
OLECULAR
BIOLOGY
METHODS
.......................................................................................
40
4.1
PREPARATION
OF
PLASMID
DEOXYRIBONUCLEIC
ACID
(DNA)
..............................................40
4.2
SITE-DIRECTED
MUTAGENESIS
BY
PCR
..........................................................................
41
4.
3
AGAROSE
GEL
ELECTROPHORESIS
.....................................................................................
42
4.4
PREPERATION
OF
CHEMICALLY
COMPETENT
E.
COLI
CELLS
....................................................
43
4.5
TRANSFORMATION
OF
CHEMICALLY
COMPETENT
E.
COLI
CELLS
..............................................
44
4.
6
SEQUENCING
OF
NUCLEIC
ACIDS
.....................................................................................
44
5
P
ROTEIN
BIOCHEMICAL
METHODS
......................................................................................
44
5.
1
DETERMINATION
OF
PROTEIN
CONCENTRATION
....................................................................
44
5.2 SODIUM
DODECYL
SULFATE
POLYACRYLAMIDE
GEL
ELECTROPHORESIS
(SDS-PAGE)
...........
46
5.2.1
STAINING
OF
SDS
GELS
USING
COOMASSIE
BRILLIANT
BLUE
........................................
47
5.2.2
STAINING
OF
SDS
GELS
USING
SILVER
STAINING
.........................................................
48
5.3
IMMUNOBLOT
................................................................................................................
49
5.3.1
SEMI-DRY
BLOTTING
SYSTEM
....................................................................................
49
5.3.2
IMMUNODETECTION
OF
PROTEINS
..............................................................................
49
5.3.3
DETECTION
OF
TAGGED
PROTEINS
BY
HRP-CONJUGATES
..............................................
51
5.
4
EUKARYOTIC
PROTEIN
EXPRESSION
..................................................................................
51
5.4.1
PROTEIN
EXPRESSION
IN
CHO
CELLS
.........................................................................
51
5.4.2
PROTEIN
EXPRESSION
IN
CHO
LEE
CELLS
.................................................................
52
5.4.3
PROTEIN
EXPRESSION
IN
COS-7
CELLS
.......................................................................
53
5.5
PURIFICATION
AND
STORAGE
OF
RECOMBINANT
PROTEINS
...................................................
54
5.5.1
IMMOBILIZED
METAL
CHELATE
AFFINITY
CHROMATOGRAPHY
(IMAC)
..............................
54
TABLE
OF
CONTENTS
5.5.2
SIZE
EXCLUSION
CHROMATOGRAPHY
(SEC)
...............................................................
54
5.5.3 BUFFER
EXCHANGE,
CONCENTRATION
AND
STORAGE
OF
PROTEIN
SOLUTIONS
.....................
55
5.5.4 PEPTIDE
SYNTHESIS
.................................................................................................
55
6
D
ETERMINATION
OF
ENZYME
ACTIVITIES
............................................................................
56
6.
1
OVASTACIN
AND
ASTACIN
INHIBITION
ASSAY
....................................................................
56
6.2
LIMITED
PROTEOLYSIS
OF
FETUINS
.....................................................................................
58
6.3
CALCIUM/PHOSPHATE
PRECIPITATE
INHIBITION
ASSAY
.......................................................
59
7
G
LYCAN
ANALYSIS
..............................................................................................................
60
7.
1
LECTIN-PROBED
WESTERN
BLOT
........................................................................................
60
7.
2
LECTIN
ENZYME-LINKED
IMMUNOSORBENT
ASSAY
(ELISA)
.............................................
60
7.
3
N-GLYCOSYLATION
FINGERPRINT
.........................................................................................
61
8
S
TATISTICAL
ANALYSIS
......................................................................................................
63
III
RESULTS
...........................................................................................................................
64
1
F
ETUIN
-B
AND
OVASTACIN
ARE
DIRECT
INTERACTION
PARTNER
DURING
FERTILIZATION
......
64
2
E
XPRESSION
CONSTRUCTS
FOR
THE
STRUCTURE
-
FUNCTION
ANALYSIS
OF
FETUIN-B
AND
OVASTACIN
..............................................................................................................................................................
66
3
S
TRUCTURE
-
FUNCTION
OF
FETUIN
-B
..................................................................................
69
3.1
FETUIN
CHIMERAS
..........................................................................................................
69
3.1.1
ANALYSIS
OF
FETUIN
CHIMERAS
FOR
FETUIN-A
ACTIVITY
.................................................
75
3.2
ORTHOLOGOUS
FETUIN
PROTEINS
.......................................................................................
76
3.3
GLYCOSYLATION
OF
FETUIN
PROTEINS
.................................................................................
78
3.3.1
N-GLYCAN
ANALYSIS
.................................................................................................
78
3.3.2
N-GLYCOSYLATION
IS
NOT
ESSENTIAL
FOR
FETUIN-B
ACTIVITY
............................................
84
4
O
PTIMIZATION
OF
OVASTACIN
EXPRESSION
IN
CHO
CELLS
................................................
86
5
C
O
-
CRYSTAL
STRUCTURE
OF
MURINE
FETUIN
-B
IN
COMPLEX
WITH
CRAYFISH
ASTACIN
......
94
IV
DISCUSSION
....................................................................................................................
104
1
F
ETUIN
-B
AND
OVASTACIN
ARE
DIRECT
INTERACTION
PARTNER
DURING
FERTILIZATION
...
104
2
P
RODUCTION
AND
ANALYSIS
OF
FETUIN
-
CHIMERA
AND
FETUIN
-B
POINT
MUTANTS
...........
105
3
G
LYCOSYLATION
OF
FETUIN
PROTEINS
.............................................................................
109
4
O
PTIMIZATION
OF
OVASTACIN
EXPRESSION
IN
CHO
CELLS
...............................................
111
5
C
O
-
CRYSTAL
STRUCTURE
OF
MURINE
FETUIN
-B
IN
COMPLEX
WITH
CRAYFISH
ASTACIN
....
113
6
C
ONCLUSION
AND
FUTURE
ASPECTS
................................................................................
121
V
REFERENCES
...................................................................................................................
123
VI
ABBREVIATIONS
............................................................................................................
133
VII LIST
OF
FIGURES
..........................................................................................................
135
VIII
LIST
OF
TABLES
..........................................................................................................
138
IX
APPENDIX
........................................................................................................................
139
1
S
UPPORTING
F
IGURES
......................................................................................................
139
2
S
UPPORTING
T
ABLES
.......................................................................................................
159
ACKNOWLEDGMENT
.............................................................................................................
162
|
| adam_txt |
TABLE
OF
CONTENTS
SUMMARY
.
6
ZUSAMMENFASSUNG
.
8
I
INTRODUCTION
.
10
1
T
HE
C
YSTATIN
S
UPERFAMILY
.
10
1.1
CYSTATIN
STRUCTURE
AND
INHIBITORY
CHARACTERISTICS
.
12
2
F
ETUIN
FAMILY
PROTEINS
.
15
2.
1
GLYCOSYLATION
.
18
2.2
BIOLOGICAL
FUNCTION
.
21
2.2.1
BIOLOGICAL
FUNCTION
OF
FETUIN-B
IN
FERTILIZATION
.
22
3
M
ETALLOPROTEINASES
.
25
3.1
A
STANDARD
ORIENTATION
FOR
METALLOPROTEINASES
.
26
3.2
ASTACIN
PROTEINASE
FAMILY
.27
3.2.1
CRAYFISH
ASTACIN
.
28
3.2.2
OVASTACIN
.
30
II
MATERIALS
AND
METHODS
.
34
1
M
ATERIALS
.
34
1.1
CHEMICALS
.
34
1.2
DEVICES
.
34
1.3
COMPUTER
SOFTWARE
AND
DATABASES
.
35
2
A
NIMAL
EXPERIMENTS
.
36
2.
1
FETUB
AND
ASTI
GENOTYPING
.
36
2.2 GENERATION
OF
FETUB'
7
',
ASTF
7
'
DOUBLE
DEFICIENT
MICE
.38
2.3
ZONA
PELLUCIDA
DIGESTION
.38
3
C
ULTIVATION
AND
STORAGE
OF
E.
COU
CELLS
.
39
3.1
CULTURE
MEDIA
AND
ANTIBIOTICS
.
39
3.2
SUSPENSION
AND
PLATE
CULTURES
.
39
3.3
STORAGE
OF
E.
COLI
CELLS
.40
4
M
OLECULAR
BIOLOGY
METHODS
.
40
4.1
PREPARATION
OF
PLASMID
DEOXYRIBONUCLEIC
ACID
(DNA)
.40
4.2
SITE-DIRECTED
MUTAGENESIS
BY
PCR
.
41
4.
3
AGAROSE
GEL
ELECTROPHORESIS
.
42
4.4
PREPERATION
OF
CHEMICALLY
COMPETENT
E.
COLI
CELLS
.
43
4.5
TRANSFORMATION
OF
CHEMICALLY
COMPETENT
E.
COLI
CELLS
.
44
4.
6
SEQUENCING
OF
NUCLEIC
ACIDS
.
44
5
P
ROTEIN
BIOCHEMICAL
METHODS
.
44
5.
1
DETERMINATION
OF
PROTEIN
CONCENTRATION
.
44
5.2 SODIUM
DODECYL
SULFATE
POLYACRYLAMIDE
GEL
ELECTROPHORESIS
(SDS-PAGE)
.
46
5.2.1
STAINING
OF
SDS
GELS
USING
COOMASSIE
BRILLIANT
BLUE
.
47
5.2.2
STAINING
OF
SDS
GELS
USING
SILVER
STAINING
.
48
5.3
IMMUNOBLOT
.
49
5.3.1
SEMI-DRY
BLOTTING
SYSTEM
.
49
5.3.2
IMMUNODETECTION
OF
PROTEINS
.
49
5.3.3
DETECTION
OF
TAGGED
PROTEINS
BY
HRP-CONJUGATES
.
51
5.
4
EUKARYOTIC
PROTEIN
EXPRESSION
.
51
5.4.1
PROTEIN
EXPRESSION
IN
CHO
CELLS
.
51
5.4.2
PROTEIN
EXPRESSION
IN
CHO
LEE
CELLS
.
52
5.4.3
PROTEIN
EXPRESSION
IN
COS-7
CELLS
.
53
5.5
PURIFICATION
AND
STORAGE
OF
RECOMBINANT
PROTEINS
.
54
5.5.1
IMMOBILIZED
METAL
CHELATE
AFFINITY
CHROMATOGRAPHY
(IMAC)
.
54
TABLE
OF
CONTENTS
5.5.2
SIZE
EXCLUSION
CHROMATOGRAPHY
(SEC)
.
54
5.5.3 BUFFER
EXCHANGE,
CONCENTRATION
AND
STORAGE
OF
PROTEIN
SOLUTIONS
.
55
5.5.4 PEPTIDE
SYNTHESIS
.
55
6
D
ETERMINATION
OF
ENZYME
ACTIVITIES
.
56
6.
1
OVASTACIN
AND
ASTACIN
INHIBITION
ASSAY
.
56
6.2
LIMITED
PROTEOLYSIS
OF
FETUINS
.
58
6.3
CALCIUM/PHOSPHATE
PRECIPITATE
INHIBITION
ASSAY
.
59
7
G
LYCAN
ANALYSIS
.
60
7.
1
LECTIN-PROBED
WESTERN
BLOT
.
60
7.
2
LECTIN
ENZYME-LINKED
IMMUNOSORBENT
ASSAY
(ELISA)
.
60
7.
3
N-GLYCOSYLATION
FINGERPRINT
.
61
8
S
TATISTICAL
ANALYSIS
.
63
III
RESULTS
.
64
1
F
ETUIN
-B
AND
OVASTACIN
ARE
DIRECT
INTERACTION
PARTNER
DURING
FERTILIZATION
.
64
2
E
XPRESSION
CONSTRUCTS
FOR
THE
STRUCTURE
-
FUNCTION
ANALYSIS
OF
FETUIN-B
AND
OVASTACIN
.
66
3
S
TRUCTURE
-
FUNCTION
OF
FETUIN
-B
.
69
3.1
FETUIN
CHIMERAS
.
69
3.1.1
ANALYSIS
OF
FETUIN
CHIMERAS
FOR
FETUIN-A
ACTIVITY
.
75
3.2
ORTHOLOGOUS
FETUIN
PROTEINS
.
76
3.3
GLYCOSYLATION
OF
FETUIN
PROTEINS
.
78
3.3.1
N-GLYCAN
ANALYSIS
.
78
3.3.2
N-GLYCOSYLATION
IS
NOT
ESSENTIAL
FOR
FETUIN-B
ACTIVITY
.
84
4
O
PTIMIZATION
OF
OVASTACIN
EXPRESSION
IN
CHO
CELLS
.
86
5
C
O
-
CRYSTAL
STRUCTURE
OF
MURINE
FETUIN
-B
IN
COMPLEX
WITH
CRAYFISH
ASTACIN
.
94
IV
DISCUSSION
.
104
1
F
ETUIN
-B
AND
OVASTACIN
ARE
DIRECT
INTERACTION
PARTNER
DURING
FERTILIZATION
.
104
2
P
RODUCTION
AND
ANALYSIS
OF
FETUIN
-
CHIMERA
AND
FETUIN
-B
POINT
MUTANTS
.
105
3
G
LYCOSYLATION
OF
FETUIN
PROTEINS
.
109
4
O
PTIMIZATION
OF
OVASTACIN
EXPRESSION
IN
CHO
CELLS
.
111
5
C
O
-
CRYSTAL
STRUCTURE
OF
MURINE
FETUIN
-B
IN
COMPLEX
WITH
CRAYFISH
ASTACIN
.
113
6
C
ONCLUSION
AND
FUTURE
ASPECTS
.
121
V
REFERENCES
.
123
VI
ABBREVIATIONS
.
133
VII LIST
OF
FIGURES
.
135
VIII
LIST
OF
TABLES
.
138
IX
APPENDIX
.
139
1
S
UPPORTING
F
IGURES
.
139
2
S
UPPORTING
T
ABLES
.
159
ACKNOWLEDGMENT
.
162 |
| any_adam_object | 1 |
| any_adam_object_boolean | 1 |
| author | Schmitz, Carlo |
| author_GND | (DE-588)1200482824 |
| author_facet | Schmitz, Carlo |
| author_role | aut |
| author_sort | Schmitz, Carlo |
| author_variant | c s cs |
| building | Verbundindex |
| bvnumber | BV046869905 |
| ctrlnum | (OCoLC)1157261007 (DE-599)DNB1207483621 |
| discipline | Biologie Medizin |
| discipline_str_mv | Biologie Medizin |
| format | Thesis Book |
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| genre | (DE-588)4113937-9 Hochschulschrift gnd-content |
| genre_facet | Hochschulschrift |
| id | DE-604.BV046869905 |
| illustrated | Illustrated |
| index_date | 2024-07-03T15:15:13Z |
| indexdate | 2024-07-10T08:56:05Z |
| institution | BVB |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-032280064 |
| oclc_num | 1157261007 |
| open_access_boolean | |
| owner | DE-355 DE-BY-UBR |
| owner_facet | DE-355 DE-BY-UBR |
| physical | 163 Seiten Illustrationen 21 cm |
| publishDate | 2019 |
| publishDateSearch | 2019 |
| publishDateSort | 2019 |
| record_format | marc |
| spelling | Schmitz, Carlo Verfasser (DE-588)1200482824 aut Structure and function of the plasma protein fetuin-B vorgelegt von M. Sc. Carlo Schmitz Aachen [2019] 163 Seiten Illustrationen 21 cm txt rdacontent n rdamedia nc rdacarrier Dissertation RWTH Aachen 2019 (DE-588)4113937-9 Hochschulschrift gnd-content B:DE-101 application/pdf https://d-nb.info/1207483621/04 Inhaltsverzeichnis DNB Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=032280064&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Schmitz, Carlo Structure and function of the plasma protein fetuin-B |
| subject_GND | (DE-588)4113937-9 |
| title | Structure and function of the plasma protein fetuin-B |
| title_auth | Structure and function of the plasma protein fetuin-B |
| title_exact_search | Structure and function of the plasma protein fetuin-B |
| title_exact_search_txtP | Structure and function of the plasma protein fetuin-B |
| title_full | Structure and function of the plasma protein fetuin-B vorgelegt von M. Sc. Carlo Schmitz |
| title_fullStr | Structure and function of the plasma protein fetuin-B vorgelegt von M. Sc. Carlo Schmitz |
| title_full_unstemmed | Structure and function of the plasma protein fetuin-B vorgelegt von M. Sc. Carlo Schmitz |
| title_short | Structure and function of the plasma protein fetuin-B |
| title_sort | structure and function of the plasma protein fetuin b |
| topic_facet | Hochschulschrift |
| url | https://d-nb.info/1207483621/04 http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=032280064&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
| work_keys_str_mv | AT schmitzcarlo structureandfunctionoftheplasmaproteinfetuinb |
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Inhaltsverzeichnis