136
J. J. GORMAN et al.
ron based analysis under conditions whereby peptide backbone cleavages were
observed. Precedence would have indicated that this interchain disulfide bond
should not have been so stable (Crimmins et al. 1995; Hemling et al. 1996; Patterson and Katta 1994; Zhou et al. 1993).
Data derived with PMP derivatives of oligo saccharides suggests that MALDIPSD of these derivatives will be of use in characterizing protein glycans.
The data reviewed herein indicate that the utility of MALDI-PSD should be
assessed in a problem specific context and precedents or dogma should not rule
out consideration of the use of PSD in particular circumstances.
5
Acknowledgments
Data depicted in figures 8.4 and 8.5 and table 8.2 were reproduced in adapted
form with permission from (Lopaticki et al. 1998; Copyright, John Wiley + Sons)
and data depicted in figures 8.6, 8.8 and 8.9 and table 8.3 were reproduced in
adapted form with permission from (Gorman et al. 1997)
References
Barber M, Bordoli RS, Elliot GJ, Sedgwick RD, Tyler AN, Green BN (1982) Fast atom bombardment of
bovine insulin and other large peptides. J Chern Soc Chern Commun 936-938
Barber M, Bordoli RS, Sedgwick RD, Tyler AN (1981) Fast atom bombardment of solids (FAB): a new
ion source for mass spectrometry. J Chern Soc Chern Commun 325-327
Bean MF, Carr SA (1992) Characterization of disulfide positions in proteins and sequence analysis of
cystine-bridged peptides by tandem mass spectrometry. Anal Biochem 201: 216-226
Biemann K (1990) The utility of mass spectrometry for the determination of the structure of peptides
and proteins. In: McEwen CN, Larsen BS (eds) Mass Spectrometry of Biological Materials. Marcel
Dekker Inc., New York, pp 3-24
Carr SA, Roberts GD, Hemling ME (1990) Structural analysis of posttranslationally modified proteins
by mass spectrometry. In: McEwen CN, Larsen BS (eds) Mass Spectrometry of Biological Materials.
Marcel Dekker Inc., New York, pp 87 -136
Collins PL, McIntosh K, Chanock RM (1996) Respiratory syncytial virus. In: Fields BN, Knipe DM,
Howley PM (eds) Virology. Lippincott-Raven Publishers, Philadelphia, pp 103 -161
Crimmins DL, Saylor M, Rush J, Thoma RS (1995) Facile, in situ matrix-assisted laser desorption
ionization-mass spectrometry analysis and assignment of disulfide bond pairings in heteropeptide
molecules. Anal Biochem 226: 355-361
Desiderio DM, Katakuse I (1983) fast atom bombardment-collision activated dissociation-linked field
scanning mass spectrometry of neuropeptide substance P. Anal. Biochem. 129: 425-429
Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM (1989) Electrospray Ionization for Mass Spectrometry of Large Biomolecules. Science 246: 64- 71
Glickman RL, Syddall RJ, Iorio RM, Sheehan JP, Bratt MA (1988) Quantiative basic residue requirements in the cleavage-activation site of the fusion glycoprotein as a determinant of virulence of
Newcastle disease virus. J Virol 62: 354-356
Gorman JJ, Corino GL, Mitchell SJ (1987) Fluorescent labeling of cysteinyl residues: Application to
extensive primary structure analysis of proteins on a micro scale. Eur J Biochem 168: 169-179
Gorman JJ, Corino GL, Selleck PW (1990a) Comparison of the positions and efficiency of cleavage
activation of fusion protein precursors of virulent and avirulent strains of Newcastle disease virus:
insights into the specificities of activating proteases. ViroI177: 339-351
Gorman JJ, Corino GL, Shiell BJ (1 990b) Role of mass spectrometry in mapping strain variation and
post-translational modifications of viral proteins. Biomed Environ Mass Spectrom 19: 646-654
Gorman JJ, Ferguson BL, Nguyen TN (1996) Use of2,6-dihydroxyacetophenone for analysis offragile
pep tides, disulfide bonding and small proteins by matrix-assisted laser desorption/ionization.
Rapid Commun Mass Spectrom 10: 529-536
J. J. GORMAN et al.
ron based analysis under conditions whereby peptide backbone cleavages were
observed. Precedence would have indicated that this interchain disulfide bond
should not have been so stable (Crimmins et al. 1995; Hemling et al. 1996; Patterson and Katta 1994; Zhou et al. 1993).
Data derived with PMP derivatives of oligo saccharides suggests that MALDIPSD of these derivatives will be of use in characterizing protein glycans.
The data reviewed herein indicate that the utility of MALDI-PSD should be
assessed in a problem specific context and precedents or dogma should not rule
out consideration of the use of PSD in particular circumstances.
5
Acknowledgments
Data depicted in figures 8.4 and 8.5 and table 8.2 were reproduced in adapted
form with permission from (Lopaticki et al. 1998; Copyright, John Wiley + Sons)
and data depicted in figures 8.6, 8.8 and 8.9 and table 8.3 were reproduced in
adapted form with permission from (Gorman et al. 1997)
References
Barber M, Bordoli RS, Elliot GJ, Sedgwick RD, Tyler AN, Green BN (1982) Fast atom bombardment of
bovine insulin and other large peptides. J Chern Soc Chern Commun 936-938
Barber M, Bordoli RS, Sedgwick RD, Tyler AN (1981) Fast atom bombardment of solids (FAB): a new
ion source for mass spectrometry. J Chern Soc Chern Commun 325-327
Bean MF, Carr SA (1992) Characterization of disulfide positions in proteins and sequence analysis of
cystine-bridged peptides by tandem mass spectrometry. Anal Biochem 201: 216-226
Biemann K (1990) The utility of mass spectrometry for the determination of the structure of peptides
and proteins. In: McEwen CN, Larsen BS (eds) Mass Spectrometry of Biological Materials. Marcel
Dekker Inc., New York, pp 3-24
Carr SA, Roberts GD, Hemling ME (1990) Structural analysis of posttranslationally modified proteins
by mass spectrometry. In: McEwen CN, Larsen BS (eds) Mass Spectrometry of Biological Materials.
Marcel Dekker Inc., New York, pp 87 -136
Collins PL, McIntosh K, Chanock RM (1996) Respiratory syncytial virus. In: Fields BN, Knipe DM,
Howley PM (eds) Virology. Lippincott-Raven Publishers, Philadelphia, pp 103 -161
Crimmins DL, Saylor M, Rush J, Thoma RS (1995) Facile, in situ matrix-assisted laser desorption
ionization-mass spectrometry analysis and assignment of disulfide bond pairings in heteropeptide
molecules. Anal Biochem 226: 355-361
Desiderio DM, Katakuse I (1983) fast atom bombardment-collision activated dissociation-linked field
scanning mass spectrometry of neuropeptide substance P. Anal. Biochem. 129: 425-429
Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM (1989) Electrospray Ionization for Mass Spectrometry of Large Biomolecules. Science 246: 64- 71
Glickman RL, Syddall RJ, Iorio RM, Sheehan JP, Bratt MA (1988) Quantiative basic residue requirements in the cleavage-activation site of the fusion glycoprotein as a determinant of virulence of
Newcastle disease virus. J Virol 62: 354-356
Gorman JJ, Corino GL, Mitchell SJ (1987) Fluorescent labeling of cysteinyl residues: Application to
extensive primary structure analysis of proteins on a micro scale. Eur J Biochem 168: 169-179
Gorman JJ, Corino GL, Selleck PW (1990a) Comparison of the positions and efficiency of cleavage
activation of fusion protein precursors of virulent and avirulent strains of Newcastle disease virus:
insights into the specificities of activating proteases. ViroI177: 339-351
Gorman JJ, Corino GL, Shiell BJ (1 990b) Role of mass spectrometry in mapping strain variation and
post-translational modifications of viral proteins. Biomed Environ Mass Spectrom 19: 646-654
Gorman JJ, Ferguson BL, Nguyen TN (1996) Use of2,6-dihydroxyacetophenone for analysis offragile
pep tides, disulfide bonding and small proteins by matrix-assisted laser desorption/ionization.
Rapid Commun Mass Spectrom 10: 529-536