130
a.i.
1200
1000
800
600
400
200
o
1400
1200
1000
800
600
400
200
o
A
NFVPCSICSNNPTCW
"
,
"
,
L ______ J ____ , ___________ I
, ,
AICK
J. J. GORMAN et al.
2115.5
2097.5
B
NFVPCSICSNNPTCWAICK
I
I
I
I
I
I
I
I
L ______ J __ __________ ____ L _______ _ J
2000
2020
2040
2060
2080
2100
2120 mlz
Flg. 8.7. Parent ion masses of (A) two chain and (B) single chain peptides obtained from the tryptic
peptide defined in Fig. 8.5 by peptic digestion and HPLC. Broken lines are used to indicate involvement of the cysteines in undefined disulfide bonds. Chemical reduction of these peptides resulted in
loss of the mass of the AICK sequence and gain of 3 for the two chain peptide and an increase of 4 in
m/z for the single chain peptide. These spectra were collected using continuous extraction and a digitization rate of 250 MHz
a.i.
1200
1000
800
600
400
200
o
1400
1200
1000
800
600
400
200
o
A
NFVPCSICSNNPTCW
"
,
"
,
L ______ J ____ , ___________ I
, ,
AICK
J. J. GORMAN et al.
2115.5
2097.5
B
NFVPCSICSNNPTCWAICK
I
I
I
I
I
I
I
I
L ______ J __ __________ ____ L _______ _ J
2000
2020
2040
2060
2080
2100
2120 mlz
Flg. 8.7. Parent ion masses of (A) two chain and (B) single chain peptides obtained from the tryptic
peptide defined in Fig. 8.5 by peptic digestion and HPLC. Broken lines are used to indicate involvement of the cysteines in undefined disulfide bonds. Chemical reduction of these peptides resulted in
loss of the mass of the AICK sequence and gain of 3 for the two chain peptide and an increase of 4 in
m/z for the single chain peptide. These spectra were collected using continuous extraction and a digitization rate of 250 MHz