Peptide fingerprints after partial acid hydrolysis: Analysis by matrix-assisted laser desorption/ionization mass spectrometry

Knierman, Michael D. ; Coligan, John E. ; Parker, Kenneth C. ; Chait, B. T.

New York, NY : Wiley-Blackwell
Published 1994
ISSN:
0951-4198
Keywords:
Chemistry ; Analytical Chemistry and Spectroscopy
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Physics
Notes:
A method is described by which a sequence-dependent peptide fingerprint can be rapidly obtained upon partial hydrolysis of peptides with hydrochloric acid and subsequent analysis by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). When synthetic peptides are treated with 3M HCI for 5 min at 110°C, amino acids are released in turn from the C-terminus or, depending on the peptide, from the N-terminus. Sequence information can be deduced by identifying the amino acid whose mass corresponds to the difference in MW between the major hydrolysis products, beginning from the MW of the starting peptide. A similar pattern exclusively from the C-terminus has been obtained using pentafluoropropionic acid as a hydrolyzing agent (Tsugita et al. Eur. J. Biochem. 206, 691 (1992)), but required longer hydrolysis time and more handling prior to analysis. The technique we have developed could be used to obtain a sequence-dependent ‘fingerprint’ for a peptide cheaply and rapidly, starting with picomole amounts of peptide, because the hydrolysate can be directly analyzed by MALDI. This methodology might be especially useful for confirming the identity of peptides during peptide mapping.
Additional Material:
1 Ill.
Type of Medium:
Electronic Resource
URL:
_version_ 1798297770384162816
addmaterial 1 Ill.
autor Knierman, Michael D.
Coligan, John E.
Parker, Kenneth C.
Chait, B. T.
autorsonst Knierman, Michael D.
Coligan, John E.
Parker, Kenneth C.
Chait, B. T.
book_url http://dx.doi.org/10.1002/rcm.1290081220
datenlieferant nat_lic_papers
hauptsatz hsatz_simple
identnr NLM159129214
iqvoc_descriptor_title iqvoc_00000708:Analysis
issn 0951-4198
journal_name Rapid Communications in Mass Spectrometry
materialart 1
notes A method is described by which a sequence-dependent peptide fingerprint can be rapidly obtained upon partial hydrolysis of peptides with hydrochloric acid and subsequent analysis by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). When synthetic peptides are treated with 3M HCI for 5 min at 110°C, amino acids are released in turn from the C-terminus or, depending on the peptide, from the N-terminus. Sequence information can be deduced by identifying the amino acid whose mass corresponds to the difference in MW between the major hydrolysis products, beginning from the MW of the starting peptide. A similar pattern exclusively from the C-terminus has been obtained using pentafluoropropionic acid as a hydrolyzing agent (Tsugita et al. Eur. J. Biochem. 206, 691 (1992)), but required longer hydrolysis time and more handling prior to analysis. The technique we have developed could be used to obtain a sequence-dependent ‘fingerprint’ for a peptide cheaply and rapidly, starting with picomole amounts of peptide, because the hydrolysate can be directly analyzed by MALDI. This methodology might be especially useful for confirming the identity of peptides during peptide mapping.
package_name Wiley-Blackwell
publikationsjahr_anzeige 1994
publikationsjahr_facette 1994
publikationsjahr_intervall 8009:1990-1994
publikationsjahr_sort 1994
publikationsort New York, NY
publisher Wiley-Blackwell
reference 8 (1994), S. 1007-1010
schlagwort Chemistry
Analytical Chemistry and Spectroscopy
search_space articles
shingle_author_1 Knierman, Michael D.
Coligan, John E.
Parker, Kenneth C.
Chait, B. T.
shingle_author_2 Knierman, Michael D.
Coligan, John E.
Parker, Kenneth C.
Chait, B. T.
shingle_author_3 Knierman, Michael D.
Coligan, John E.
Parker, Kenneth C.
Chait, B. T.
shingle_author_4 Knierman, Michael D.
Coligan, John E.
Parker, Kenneth C.
Chait, B. T.
shingle_catch_all_1 Knierman, Michael D.
Coligan, John E.
Parker, Kenneth C.
Chait, B. T.
Peptide fingerprints after partial acid hydrolysis: Analysis by matrix-assisted laser desorption/ionization mass spectrometry
Chemistry
Analytical Chemistry and Spectroscopy
Chemistry
Analytical Chemistry and Spectroscopy
A method is described by which a sequence-dependent peptide fingerprint can be rapidly obtained upon partial hydrolysis of peptides with hydrochloric acid and subsequent analysis by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). When synthetic peptides are treated with 3M HCI for 5 min at 110°C, amino acids are released in turn from the C-terminus or, depending on the peptide, from the N-terminus. Sequence information can be deduced by identifying the amino acid whose mass corresponds to the difference in MW between the major hydrolysis products, beginning from the MW of the starting peptide. A similar pattern exclusively from the C-terminus has been obtained using pentafluoropropionic acid as a hydrolyzing agent (Tsugita et al. Eur. J. Biochem. 206, 691 (1992)), but required longer hydrolysis time and more handling prior to analysis. The technique we have developed could be used to obtain a sequence-dependent ‘fingerprint’ for a peptide cheaply and rapidly, starting with picomole amounts of peptide, because the hydrolysate can be directly analyzed by MALDI. This methodology might be especially useful for confirming the identity of peptides during peptide mapping.
0951-4198
09514198
Wiley-Blackwell
shingle_catch_all_2 Knierman, Michael D.
Coligan, John E.
Parker, Kenneth C.
Chait, B. T.
Peptide fingerprints after partial acid hydrolysis: Analysis by matrix-assisted laser desorption/ionization mass spectrometry
Chemistry
Analytical Chemistry and Spectroscopy
Chemistry
Analytical Chemistry and Spectroscopy
A method is described by which a sequence-dependent peptide fingerprint can be rapidly obtained upon partial hydrolysis of peptides with hydrochloric acid and subsequent analysis by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). When synthetic peptides are treated with 3M HCI for 5 min at 110°C, amino acids are released in turn from the C-terminus or, depending on the peptide, from the N-terminus. Sequence information can be deduced by identifying the amino acid whose mass corresponds to the difference in MW between the major hydrolysis products, beginning from the MW of the starting peptide. A similar pattern exclusively from the C-terminus has been obtained using pentafluoropropionic acid as a hydrolyzing agent (Tsugita et al. Eur. J. Biochem. 206, 691 (1992)), but required longer hydrolysis time and more handling prior to analysis. The technique we have developed could be used to obtain a sequence-dependent ‘fingerprint’ for a peptide cheaply and rapidly, starting with picomole amounts of peptide, because the hydrolysate can be directly analyzed by MALDI. This methodology might be especially useful for confirming the identity of peptides during peptide mapping.
0951-4198
09514198
Wiley-Blackwell
shingle_catch_all_3 Knierman, Michael D.
Coligan, John E.
Parker, Kenneth C.
Chait, B. T.
Peptide fingerprints after partial acid hydrolysis: Analysis by matrix-assisted laser desorption/ionization mass spectrometry
Chemistry
Analytical Chemistry and Spectroscopy
Chemistry
Analytical Chemistry and Spectroscopy
A method is described by which a sequence-dependent peptide fingerprint can be rapidly obtained upon partial hydrolysis of peptides with hydrochloric acid and subsequent analysis by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). When synthetic peptides are treated with 3M HCI for 5 min at 110°C, amino acids are released in turn from the C-terminus or, depending on the peptide, from the N-terminus. Sequence information can be deduced by identifying the amino acid whose mass corresponds to the difference in MW between the major hydrolysis products, beginning from the MW of the starting peptide. A similar pattern exclusively from the C-terminus has been obtained using pentafluoropropionic acid as a hydrolyzing agent (Tsugita et al. Eur. J. Biochem. 206, 691 (1992)), but required longer hydrolysis time and more handling prior to analysis. The technique we have developed could be used to obtain a sequence-dependent ‘fingerprint’ for a peptide cheaply and rapidly, starting with picomole amounts of peptide, because the hydrolysate can be directly analyzed by MALDI. This methodology might be especially useful for confirming the identity of peptides during peptide mapping.
0951-4198
09514198
Wiley-Blackwell
shingle_catch_all_4 Knierman, Michael D.
Coligan, John E.
Parker, Kenneth C.
Chait, B. T.
Peptide fingerprints after partial acid hydrolysis: Analysis by matrix-assisted laser desorption/ionization mass spectrometry
Chemistry
Analytical Chemistry and Spectroscopy
Chemistry
Analytical Chemistry and Spectroscopy
A method is described by which a sequence-dependent peptide fingerprint can be rapidly obtained upon partial hydrolysis of peptides with hydrochloric acid and subsequent analysis by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). When synthetic peptides are treated with 3M HCI for 5 min at 110°C, amino acids are released in turn from the C-terminus or, depending on the peptide, from the N-terminus. Sequence information can be deduced by identifying the amino acid whose mass corresponds to the difference in MW between the major hydrolysis products, beginning from the MW of the starting peptide. A similar pattern exclusively from the C-terminus has been obtained using pentafluoropropionic acid as a hydrolyzing agent (Tsugita et al. Eur. J. Biochem. 206, 691 (1992)), but required longer hydrolysis time and more handling prior to analysis. The technique we have developed could be used to obtain a sequence-dependent ‘fingerprint’ for a peptide cheaply and rapidly, starting with picomole amounts of peptide, because the hydrolysate can be directly analyzed by MALDI. This methodology might be especially useful for confirming the identity of peptides during peptide mapping.
0951-4198
09514198
Wiley-Blackwell
shingle_title_1 Peptide fingerprints after partial acid hydrolysis: Analysis by matrix-assisted laser desorption/ionization mass spectrometry
shingle_title_2 Peptide fingerprints after partial acid hydrolysis: Analysis by matrix-assisted laser desorption/ionization mass spectrometry
shingle_title_3 Peptide fingerprints after partial acid hydrolysis: Analysis by matrix-assisted laser desorption/ionization mass spectrometry
shingle_title_4 Peptide fingerprints after partial acid hydrolysis: Analysis by matrix-assisted laser desorption/ionization mass spectrometry
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geomar
wilbert
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albert
source_archive Wiley InterScience Backfile Collection 1832-2000
timestamp 2024-05-06T10:13:14.576Z
titel Peptide fingerprints after partial acid hydrolysis: Analysis by matrix-assisted laser desorption/ionization mass spectrometry
titel_suche Peptide fingerprints after partial acid hydrolysis: Analysis by matrix-assisted laser desorption/ionization mass spectrometry
topic U
uid nat_lic_papers_NLM159129214