Supplementary Table S2: Identified Tear proteins and their functions
Spot
ID
1.
2.
3.
4.
5.
6.
Identified
Tear proteins
Database/
Accession
no.
Mowse
scorea
Mammaglobin-B Swissprot/SG 255 (29)
precursor
2A1_HUMA
N
Cystatin SA III
NCBI/
105 (27)
potential
gi|235948
precursor
of
acquired
enemal
Cystatin
S
NCBI/
60 (35)
precursor
gi|4503109
Lysozyme-C
MSDB/LZ 81 (34)
precursor
HU
Cystatin
precursor
S
MSDB / 495 (36)
UDHUP1
Chain B,crystal
structure of
component
formed
NCBI/gi|21
between Mhc
0061077
like Zn alpha 2
glycoprotein
and PIP
X&Y
coordinate
in DIGE
gel
105,940
92,920
Mr/ pI
2-Db
< 14/5.1
14/4.5
Mr/ pI data
basec
10.8/5.48
14.1/4.74
Peptides Matchedd
K.LLEDMVEK.T
K.TINSDISIPEYK.E
K.ELLQEFIDSDAAAEAMGK.F
R.IIPGGIYDADLNDEWVQR.A
R.ALHFAISEYNK.A
K.ATEDEYYR.R R.RPLQVLR.A
R.EQTFGGVNYFFDVEVGR.T
K.SQPNLDTCAFHEQPELQK.K
K.QLCSFEIYEVPWEDR.M
166,875
16/4.6
16.2/ 4.95
R.ALHFAISEYNK.A
190,869
16/4.7
16.5/9.3
R.STDYGIFQINSR.Y
Sequence
Coverage
(%)e
40
303 (38) 375,870
16/4.8
14/5
16.2/ 4.95
77
7
13.5/5.4
R.IIPGGIYDADLNDEWVQR.A
R.ALHFAISEYNK.A
K.ATEDEYYRRPLQVLR.A
K.SQPNLDTCAFHEQPELQK.K
K.KQLCSFEIYEVPWEDR.M
K.QLCSFEIYEVPWEDR.M
K.IIIKNFDIPK.S K.NFDIPK.S
K.YTACLCDDNPK.T
K.TFYWDFYTNR.T
R.TVQIAAVVDVIR.E
R.FYTIEILKVE.-
To bind androgens
and other steroids
Cysteine protease
inhibitor
8
242,870
Function
55
44
Cysteine protease
inhibitor
Hydrolyzes
polysaccharides
found in many
bacterial cell walls
Cysteine protease
inhibitor
unknown
7.
8.
9.
10.
11.
Lipocalin
precursor
1
NCBI
112 (28)
/gi|450496
3
NCBI / 107 (36)
gi|6730358
Chain A, Role
Of
Amino
Acid Residues
At Turns In
The
Conformationa
l Stability And
Folding
Of
Human
Lysozyme
Transthyretin
Swissprot / 361 (27)
OS=Homo
TTHY_HU
sapiens
MAN
GN=TTR
PE=1 SV=1
cystatin SAIII=potential
precursor of
acquired
enamel
pellicle
[human,
Peptide, 121
aa]
NCBI/gi|2
35948
Transthyretin
OS=Homo
sapiens
GN=TTR
Swissprot/
TTHY_HU
MAN
474,909
453,830
14/5.2
14/5.5
19.2/5.39
14.9 / 9.14
12
K.RLGMDGYR.G R.LGMDGYR.G
R.STDYGIFQINSR.Y
K.RVVDPQGIR.A R.AWVAWR.N
Lipid scavenging
and transport to
outer tear layer
Hydrolyzes
polysaccharides
found in many
bacterial cell walls
27
478,811
14/5.7
15.9/5.52
182(38) 484,835
16/5.4
14.1/4.7
536,835
14/5.8
15.8/5.52
60(27)
K.NNLEALEDFEK.A
R.GLSTESILIPR.Q
R.GSPAINVAVHVFR.K
R.GSPAINVAVHVFRK.A
R.GSPAINVAVHVFRK.A
R.KAADDTWEPFASGK.T
K.AADDTWEPFASGK.T
R.IIPGGIYDADLNDEWVQR.A
R.RPLQVLR.A
K.SQPNLDTCAFHEQPELQK.KK.S
QPNLDTCAFHEQPELQK.K
R.GSPAINVAVHVFR.K
18
Binds retinol to
retinol-binding
protein
35
Cysteine protease
inhibitor
8
Binds retinol to
retinol-binding
protein
PE=1 SV=1
12.
13.
14.
15.
Chain A,
Cyrstal
structure of
Human tear
lipocalinVON
EBNERS
GLAND
Protein
alpha-1-Bglycoprotein human
NCBI/
125 (37)
gi|5655458
4
566,892
14/5.7
17.9/5.27
K.VTMLISGR.C
K.YTADGGKHVAYIIR.S
K.HVAYIIR.S R.GLSTESILIPR.Q
Lipid scavenging
and transport to
outer tear layer
20
408(38)
717,882.
15/6.3
51.9/5.6
698,919
13/6.5
16.3/6.8
728,917
< 14/6.5
NCBI/gi|69
990
RecName:
Full=CystatinSN; AltName:
Full=Cystatin1; AltName:
Full=Salivary
cystatin-SA-1;
AltName:
Full=CystainSA-I; Flags:
Precursor
NCBI/gi|33
7752
Beta-2Microglobulin
precursor
Swissprot// 59 (28)
B2MG_HU
MAN
42(37)
13.8/6.06
R.LETPDFQLFK.N
K.LLELTGPK.S K.LLELTGPK.S
K.LLELTGPK.S K.LLELTGPK.S
R.GVTFLLR.R
K.VTLTCVAPLSGVDFQLR.R
K.VTLTCVAPLSGVDFQLRR.G
K.ELLVPR.S R.CLAPLEGAR.F
R.LELHVDGPPPRPQLR.A
R.CEGPIPDVTFELLR.E
R.TPGAAANLELIFVGPQHAGNY
R.C
K.SQPNLDTCAFHEQPELQK.K
22
Unknown
12
Cysteine protease
inhibitor
R.IEKVEHSDLSFSK.D
R.VNHVTLSQPK.I
19
Presentation of
peptide antigens to
the immune
system.
16.
17.
18.
19.
20.
21.
22.
Cystatin
precursor
SN NCBI/
66 (55)
gi|1988225
1
Mutant
lysozyme
827,902
121(36) 765,770
15.7/8.48 16.3/ 6.7
14.3/6.7
14.6/9.3
NCBI/gi|18
27553
Haptoglobin
Swissprot / 163 (27)
OS=Homo
HPT_HUM
sapiens
AN
GN=HP PE=1
SV=1 – α2
chain (R)
Haptoglobin
Swissprot 212 (35)
OS=Homo
HPT_HU
sapiens
MAN
GN=HP PE=1
SV=1 α2 chain
(M)
Haptoglobin
Swissprot / 168 (27)
OS=Homo
HPT_HUM
sapiens
AN
GN=HP PE=1
SV=1 α2 chain
(L)
Lacrimal
MSDB/ 394 (35)
lipocalin
LCHUL
precursor
671,736
Human
lipocalin
340,731
tear
NCBI/
72 (64)
gi|5655458
21/6.0
45.8/6.1
R.IIPGGIYNADLNDEWVQR.A
R.QQTVGGVNYFFDVEVGR.T
K.SQPNLDTCAFHEQPELQK.K
K.KQLCSFEIYEVPWENR.R
K.QLCSFEIYEVPWENR.R
K.QLCSFEIYEVPWENRR.S
R.LGMDGYR.G
R.STDYGIFQINSR.Y
R.AWVAWR.N
49
19
K.NYYKLR.T
K.LRTEGDGVYTLNNEK.Q
R.TEGDGVYTLNNEK.Q
R.TEGDGVYTLNNEKQWINK.A
Cysteine protease
inhibitor
Hydrolyzes
polysaccharides
found in many
bacterial cell walls
Haeme binding
protein
6
555,724
20/5.9
45.8/6.1
K.NYYKLR.T
K.LRTEGDGVYTLNNEK.Q
R.TEGDGVYTLNNEK.Q
R.TEGDGVYTLNNEKQWINK.A
Haeme binding
protein
6
450,730
21/5.5
45.8/6.1
K.LRTEGDGVYTLNNEK.Q
R.TEGDGVYTLNNEK.Q
R.TEGDGVYTLNNEKQWINK.A
Haeme binding
protein
4
406,750
18/5.3
19.2/5.39
18.3/4.76 17.9/5.27
K.VTMLISGR.C
K.DHYIFYCEGELHGKPVR.G
K.NNLEALEDFEK.A
K.NNLEALEDFEKAAGAR.G
R.GLSTESILIPR.Q
R.EFPEMNLESVTPMTLTTLEGG
NLEAK.V K.HVAYIIR.S
K.NNLEALEDFEK.A
R.GLSTESILIPR.Q
29
Lipid scavenging
and transport to
outer tear layer
33
Lipid scavenging
and transport to
4
23.
24.
25.
26.
27.
Prolactin
inducible
protein
outer tear layer
NCBI/
92 (64)
gi|4505821
Lacrimal
lipocalin
precursor
Full putative
lipocalin 1 like
protein
Prolactininducible
protein
MSDB/
LCHUL
112 (36)
Swissprot/ 85 (28)
LC1L1_H
UMAN
Swissprot/ 546 (29)
PIP_HUM
AN
244,727
174,733
121,756
19/4.4
20/4.8
16.5/8.2
19.2/5.39
17.9/4.93
174,785
20/4.8
20/4.8
16.8/8.2
19.3/5.2
NCBI/gi|11
9608459
28.
29.
30.
PIP precursor
Ig Kappa
light chain
Lacritin
Precursor
1
K.SVRPNDEVTAVLAVQTELK.E
K.TYLISSIPLQGAFNYK.Y
K.YTACLCDDNPK.T
R.TVQIAAVVDVIR.E
R.ELGICPDDAAVIPIK.N
R.FYTIEILK.V
K.NNLEALEDFEK.A
R.GLSTESILIPR.Q
55
12
R.GLSTESILIPR.Q
6
160 (26) 195,781
hCG 201503
20/4.24
NCBI/gi|45 134 (32)
05821
221,783
NCBI/
163 (37)
gi|1706844
04
NCBI/ 62 (38)
gi|1518716
4
240,788
244,622
20/5.2
20/5.2
26/4.8
16.5/8.2
23.5/6.08
14.2/5.43
R.KIIIKNFDIPK.S
K.IIIKNFDIPK.S K.NFDIPK.S
K.SVRPNDEVTAVLAVQTELKEC
MVVK.T
K.TYLISSIPLQGAFNYK.Y
K.YTACLCDDNPK.T
R.TVQIAAVVDVIR.E
R.ELGICPDDAAVIPIK.N
R.ELGICPDDAAVIPIKNNR.F
K.NNRFYTIEILKVE
R.FYTIEILK.V R.FYTIEILKVE
K.HVAYIIR.S
K.LVGRDPENNLEALEDFEK.A
R.GLSTESILIPR.Q
R.GLSTESILIPRQSETCSPGSD.-
K.NFDIPK.S K.YTACLCDDNPK.T
R.TVQIAAVVDVIR.E
R.ELGICPDDAAVIPIK.N
R.FYTIEILK.V
R.TVAAPSVFIFPPSDEQLK.S
K.DSTYSLSSTLTLSK.A
K.VYACEVTHQGLSSPVTK.S
K.SILLTEQALAK.A
K.KFSLLKPWA
Suppressing T-cell
apoptosis
Lipid scavenging
and transport to
outer tear layer
Lipid scavenging
and transport to
outer tear layer
Suppressing T-cell
apoptosis
70
26
unknown
35
Suppressing T-cell
apoptosis
Antigen Binding
22
14
Secretion,
renewal of
lacrimal & ocular
31.
32.
33.
34.
35.
36.
37.
38.
Lacritin
precursor
NCBI/
62 (38)
gi|1518716
4
373,627
Pro
Apolipoprotei
n
Chain
A,
Crystal
Structure
Of
Lipid-Free
Human
Apolipoprotein
A-I
NCBI/gi|1 204 (27)
78775
367,575
NCBI / 507 (36)
gi|9010866
4
399,574
Ig alpha
apolipoprotein
E [Homo
sapiens]
Swissprot/ 86 (28)
IGHA1_H
UMAN
26/5.3
14.2/5.4
14
749,241
30/5.2
29/5.1
28.9/5.45
28/5.2
38.4/6.08 45/6.2
32/5.5
36.1/5.65
NCBI/gi|17
8849
MSDB/
LCHUL
142 (36)
Zn-alpha2-
NCBI/gi|3 607 (36)
86 (37)
K.LLDNWDSVTSTFSK.L
R.THLAPYSDELRQR.L
K.ATEHLSTLSEK.A
K.AKPALEDLR.Q
-.DEPPQSPWDRVK.D
R.DYVSQFEGSALGK.Q
K.LLDNWDSVTSTFSK.L
R.QEMSKDLEEVK.A
K.VEPLRAELQEGAR.Q
R.QKLHELQEK.L
K.LSPLGEEMRDR.A
R.ARAHVDALR.T
R.THLAPYSDELRQR.L
K.ATEHLSTLSEK.A
K.AKPALEDLR.Q
K.TPLTATLSK.S
R.EKYLTWASR.Q K.YLTWASR.Q
18
431,394
249,307
40/5.1
45/4.6
19.2/5.39
34.7/5.7
NCBI/gi|38
026
293,317
51/4.8
34.7/5.71
R.LGPLVEQGR.V
R.AKLEEQAQQIR.L
R.LQAEAFQAR.L
K.NNLEALEDFEK.A
R.GLSTESILIPR.Q
K.EIPAWVPFDPAAQITK.Q
K.AYLEEECPATLR.K
R.YSLTYIYTGLSK.H
K.SQPMGLWR.Q
surface epithelia
Secretion, renewal
of lacrimal &
ocular surface
epithelia
Lipid profile
regulator
Lipid profile
regulator
51
5
124(37) 509,462
Lacrimal
lipocalin
precursor
Zn-alpha2glycoprotein
[Homo
sapiens]
K.SILLTEQALAK.A
K.KFSLLKPWA.-
9
12
9
37
Major
Immunoglobulin
Class In Body
Secretions
Lipid profile
regulator
Lipid scavenging
and transport to
outer tear layer
Stimulates lipid
degradation
Stimulates lipid
glycoprotein
[Homo
sapiens]
39.
8026
Zinc-alpha-2glycoprotein
OS=Homo
sapiens
NCBI/gi|38
026
40.
Haptoglobin
precursor – β
chain
NCBI/gi|3
06882
41.
Zinc-alpha-2MSDB/1Z 213 (36) 407,353
glycoprotein,
AGA
chain
A
human
Actin,
Swissprot/ 94 (28)
397,291
cytoplasmic 1
ACTB_HU
MAN
Haptoglobin
234(38) 430,342
isoform 2 pre
NCBI/gi|18
protein - β
6910296
chain
42.
43.
44.
lactoferrin
[Homo
sapiens]
134(35)
182(35)
79 (38)
NCBI/gi|21
04522
332,317
379,336
485,337
39/5.3
34.7/5.7
39/5.6
45.1/6.24
45/5.4
39/5.5
31.5/5.70
42/5.29
40/5.7
38.4/6.1
42/5.6
52.3/7
R.QVEGMEDWK.Q
R.QVEGMEDWKQDSQLQK.A
K.AREDIFMETLK.D
R.EDIFMETLK.D
K.YYYDGKDYIEFNK.E
K.QKWEAEPVYVQR.A
K.WEAEPVYVQR.A
K.AYLEEECPATLR.K
K.AYLEEECPATLRK.Y
R.QDPPSVVVTSHQAPGEK.K
K.CLAYDFYPGK.I
R.YSLTYIYTGLSK.H
R.SSGAFWK.Y
R.AGEVQEPELR.G
R.ILGGHLDAK.G
K.GSFPWQAK.M
K.DIAPTLTLYVGK.KK.QLVEIEK.
V R.VGYVSGWGR.N K.FTDHLK.Y
K.VTSIQDWVQK.T
R.YSLTYIYTGLSK.H
K.YYYDGKDYIEFNK.E
K.AYLEEECPATLR.K
K.CLAYDFYPGK.I
K.AGFAGDDAPR.A
R.GYSFTTTAER.E K.IIAPPER.K
K.IIAPPERK.Y
K.GSFPWQAK.M
K.DIAPTLTLYVGKK.Q
K.QLVEIEK.V
K.YVMLPVADQDQCIR.H
K.SCAVAEYGVYVK.V
K.VTSIQDWVQK.T
R.KSEEEVAAR.R
K.CGLVPVLAENYK.S
R.CLAENAGDVAFVK.D
R.KPVTEAR.S
degradation
9
Stimulates lipid
degradation
15
Haeme binding
protein
17
Stimulates lipid
degradation
Structural protein
7
18
8
Haeme binding
protein
Antimicrobial
activity
45.
46.
47.
48.
ALB protein
(Growthinhibiting
protein 20).Homo sapiens
(Human).
532(36) 619,357
45/6.1
47.3/5.9
730,293
50/6.8
52/5.6
162(39) 545,273
49/5.8
47.3/5.9
513(39) 569,318
44/5.9
47.3/5.9
MSDB/Q8
6YG0_HU
MAN
206(37)
albuminNCBI/gi|76
like [Homo
3431]
sapiens
ALB protein
[Homo
sapiens]
ALB protein
[Homo
sapiens]
NCBI/gi|27
692693
NCBI/gi|27
692693
K.AWAVAR.L R.LSQRFPK.A
R.LSQRFPK.A K.AEFAEVSK.L
K.LVTDLTK.V
K.VHTECCHGDLLECADDRADLA
K.Y K.LKECCEKPLLEK.S
K.LKECCEKPLLEK.S
K.TYETTLEK.C
K.CCAAADPHECYAK.V
K.VFDEFKPLVEEPQNLIK.Q
K.QNCELFEQLGEYK.F
K.FQNALLVR.Y K.FQNALLVR.Y
K.KVPQVSTPTLVEVSR.N
K.CCKHPEAK.R K.CCKHPEAK.R
K.HPEAKR.M K.TPVSDRVTK.C
K.CCTESLVNR.R
R.RPCFSALEVDETYVPK.E
K.KQTALVELVK.H
K.KQTALVELVK.H
K.QTALVELVK.H
K.QTALVELVK.H
K.AVMDDFAAFVEK.C
K.AVMDDFAAFVEK.C
K.LVAASQAALGL.K.LVNEVTEFAK.T
K.LVNEVTEFAK.T K.YLYEIAR.R
K.LVTDLTK.V K.LVTDLTK.V
K.VHTECCHGDLLECADDRADLA
K.YK.VHTECCHGDLLECADDRA
DLAK.Y R.RHPDYSVVLLLR.L
K.QNCELFEQLGEYK.F
R.LSQRFPK.A K.LVTDLTK.V
K.LVTDLTK.V
K.KVPQVSTPTLVEVSR.N
K.KVPQVSTPTLVEVSR.N
K.KQTALVELVK.H
50
Regulation of the
colloidal osmotic
pressure of blood
15
Regulation of the
colloidal osmotic
pressure of blood
9
Regulation of the
colloidal osmotic
pressure of blood
K.AWAVAR.L R.LSQRFPK.A
K.AEFAEVSK.L K.LVTDLTK.V
K.VHTECCHGDLLECADDRADLA
K.Y K.LKECCEKPLLEK.S
K.TYETTLEK.C
K.CCAAADPHECYAK.V
K.VFDEFKPLVEEPQNLIK.Q
K.QNCELFEQLGEYK.F
K.FQNALLVR.Y
K.KVPQVSTPTLVEVSR.N
K.CCKHPEAK.R K.HPEAKR.M
K.TPVSDRVTK.C
50
Regulation of the
colloidal osmotic
pressure of blood
49.
Serum albumin
OS=Homo
sapiens
GN=ALB
PE=1 SV=2
50.
51.
Ig
alpha-1
chain C region
Ig gamma-1
chain C region
OS=Homo
sapiens
GN=IGHG1
PE=1 SV=1
52.
Lactoferrin
53.
Lactoferrin
519(29)
644,228
Swissprot/ 86 (28)
IGHA1_H
UMAN
741,237
66/6
69.3/5.92
Swissprot/
ALBU_HU
MAN
89(28)
38.4/6.08 45/6.2
K.CCTESLVNR.R
R.RPCFSALEVDETYVPK.E
K.KQTALVELVK.H
K.QTALVELVK.H
K.AVMDDFAAFVEK.C
K.LVAASQAALGL.K.LVNEVTEFAK.T
K.SLHTLFGDK.L K.LCTVATLR.E
R.NECFLQHK.D K.DDNPNLPR.L
K.KYLYEIAR.R K.YLYEIAR.R
K.AACLLPK.L K.LDELRDEGK.A
K.AWAVAR.L R.LSQRFPK.A
K.AEFAEVSK.L K.LVTDLTK.V
R.HPDYSVVLLLR.LK.TYETTLEK
.C K.FQNALLVR.Y
K.CCTESLVNR.R
K.KQTALVELVK.H
K.QTALVELVK.H
K.AVMDDFAAFVEK.C
K.KLVAASQAALGL.K.LVAASQAALGL.-
27
K.TPLTATLSK.S
R.EKYLTWASR.Q K.YLTWASR.Q
5
756,235
43/6.2
36/8.46
K.GPSVFPLAPSSK.S
K.DTLMISR.T K.ALPAPIEK.T
K.NQVSLTCLVK.G
11
Swissprot/I
GHG1_HU
MAN
NCBI/gi|2 222 (38)
104522
NCBI/gi|21 155 (28)
800,269
834,218
50/7
50/7
53.6/7.09
53.6/7
K.CGLVPVLAENYK.S
R.SDTSLTWNSVK.G
R.CLAENAGDVAFVK.D
K.CGLVPVLAENYK.S
R.SDTSLTWNSVK.G
9
7
Regulation of the
colloidal osmotic
pressure of blood
Major
Immunoglobulin
Class In Body
Secretions
Major
Immunoglobulin
Class In Body
Secretions
Antimicrobial
activity
Antimicrobial
R.CLAENAGDVAFVK.D
04522
54.
55.
56.
57.
RecName:
Full=Ig
gamma-4
chain C
region
Chain A,
Structure Of
Human
Apolactoferrin
At 2.0 A
Resolution
Serotransferrin
precursor
[Homo
sapiens]
111(36)
793,177
70/7
35.9/7.1
K.GPSVFPLAPCSR.S
R.STSESTAALGCLVK.D
K.NQVSLTCLVK.G
K.NQVSLTCLVK.G
105(38)
712,219
67/6.8
76.1/8.4
196(38)
668,181
68/6.6
1568(35)
573,82
66/6.3
activity
11
Major
Immunoglobulin
Class In Body
Secretions
R.DGAGDVAFIR.E K.DLLFK.D
R.CLAENAGDVAFVK.D
4
Antimicrobial
activity
77/6.8
K.SVIPSDGPSVACVK.K
K.SASDLTWDNLK.G
R.FDEFFSEGCAPGSK.K
K.EGYYGYTGAFR.C
7
iron-binding blood
plasma
glycoproteins
77/6.8
K.SVIPSDGPSVACVKK.A
K.ASYLDCIR.A
K.DSGFQMNQLR.G
K.CLKDGAGDVAFVK.H
K.DGAGDVAFVK.H
K.HSTIFENLANK.A
K.DCHLAQVPSHTVVAR.S
K.EFQLFSSPHGK.D
K.MYLGYEYVTAIR.N
K.CDEWSVNSVGKIECVSAETTED
CIAK.I K.IECVSAETTEDCIAK.I
K.KSASDLTWDNLK.G
K.SASDLTWDNLK.G
R.TAGWNIPMGLLYNK.I
R.FDEFFSEGCAPGSK.K
K.LCMGSGLNLCEPNNK.E
K.EGYYGYTGAFR.C
R.CLVEKGDVAFVK.H
K.NLNEKDYELLCLDGTR.K
K.DLLFR.D
35
iron-binding blood
plasma
glycoproteins
NCBI/gi|12
1047
NCBI/gi|46
99853
NCBI/gi|45
57871
transferrin
precursor
[validated] human
MSDB/TF
HUP
58.
59.
60.
61.
Serum
albumin,
chain A
Chain A,
Human Serum
Albumin In A
Complex With
Myristic Acid
And TriIodobenzoic
Acid
Unnamed
protein
Albumin,
isoform CRA
H
MSDB /
1AO6A
639 (36)
550,131
917(27) 467,135
66/5.1
66/5.6
65.6/5.63
65.9/5.69
NCBI/gi|15
7830361
NCBI /
gi|34412
162 (37)
432,192
569(28) 397,195
NCBI/gi|11
9626071
66/ 6.1
66/5.5
79.9/ 8.5
68.5/5.92
K.DLLFRDDTVCLAK.L
K.YLGEEYVK.A
R.KCSTSSLLEACTFR.R
K.CSTSSLLEACTFR.R
R.FKDLGEENFK.A
K.LVNEVTEFAK.T
K.KYLYEIAR.R K.YLYEIAR.R
K.VHTECCHGDLLECADDR.A
K.VHTECCHGDLLECADDRADLA
K.Y K.QNCELFEQLGEYK.F
K.FQNALLVR.Y
K.KVPQVSTPTLVEVSR.N
K.VPQVSTPTLVEVSR.N
K.QTALVELVK.H
K.AVMDDFAAFVEK.C
R.FKDLGEENFK.A
K.LVNEVTEFAK.T
K.SLHTLFGDK.L K.LCTVATLR.E
R.ETYGEMADCCAK.Q
K.KYLYEIAR.R K.YLYEIAR.R
K.YLYEIARR.H
K.AAFTECCQAADK.A
K.AACLLPK.L
K.YICENQDSISSK.L
K.LKECCEKPLLEK.S
K.ECCEKPLLEK.S
K.FQNALLVR.Y
K.KVPQVSTPTLVEVSR.N
K.VPQVSTPTLVEVSR.N
R.RPCFSALEVDETYVPK.E
K.KQTALVELVK.H
K.QTALVELVK.H
K.LVAASQAALG.R.VVWCAVGEQELRK.C
K.CGLVPVLAENYK.S
R.CLAENAGDVAFVK.D
R.FKDLGEENFK.A
K.LVNEVTEFAK.T
K.SLHTLFGDK.L K.LCTVATLR.E
R.ETYGEMADCCAK.Q
K.KYLYEIAR.R K.YLYEIAR.R
K.YLYEIARR.H
K.AAFTECCQAADK.A
K.AACLLPK.L
K.YICENQDSISSK.L
K.LKECCEKPLLEK.S
K.ECCEKPLLEK.S
K.FQNALLVR.Y
K.VPQVSTPTLVEVSR.N
Regulation of the
colloidal osmotic
pressure of blood
18
27
5
24
Regulation of the
colloidal osmotic
pressure of blood
Unknown
Regulation of the
colloidal osmotic
pressure of blood
62.
Chain A,
Human serum
albumin
complex with
myristic acid
and tri iodo
benzene acid
371(27) 366,199
Swissprot/g
i|15783036
1
66/5.4
65.9/5.69
K.KQTALVELVK.H
K.QTALVELVK.H
K.KLVAASQAALGL.K.LVAASQAALGL.K.DLGEENFK.A
K.LVNEVTEFAK.T
K.SLHTLFGDK.L K.LCTVATLR.E
K.YLYEIAR.R K.AACLLPK.L
K.ECCEKPLLEK.S
R.HPDYSVVLLLR.L
K.FQNALLVR.Y
K.QTALVELVK.H
K.AVMDDFAAFVEK.C
K.LVAASQAALG.-
18
Regulation of the
colloidal osmotic
pressure of blood
K.TDTSHHDQDHPTFNK.I
Swissprot 76 (28)
269,210
45/5.2
46.8/5.3
Inhibitor of serine
K.IVDLVK.E K.FLENEDRR.S
/A1AT_H
9
proteases
K.LSITGTYDLK.S
UMAN
K.TDTSHHDQDHPTFNK.I
64. Alpha-1Swissprot / 76 (28)
244,206
45/5.1
46.8/5.3
Inhibitor of serine
K.IVDLVK.E K.FLENEDRR.S
antitrypsin
A1AT_HU
9
proteases
K.LSITGTYDLK.S
MAN
a
MOWSE scores greater than the values given in the parenthesis are considered to be significant (p < 0.05). All proteins were also
searched across multiple databases to confirm their identity. bApparent/ experimental molecular weight and pI of protein spot on 2-DE
gels. cTheoretical molecular weight and pI of the identified protein in database. dRepresents the peptides matched. eSequence coverage
(SC) represents the % aminoacid sequence covered in the protein by the matched peptides. 18R, 19M and 20L of α2 isoforms are
labeled according to Gupta [22] et al.,2007. Spot 5 is of very low intensity and spot 33 is a highly abundant protein. Under our
conditions both give vey high MOWSE scores.
63.
Alpha-1antitrypsin