FAST ATOM BOMBARDMENT MASS SPECTROMETRY (FABMS) ANALYSIS OF AN N- TERMINAL - BLOCKED PEPTIDE

FABMS analysis of T-lb peptide before and after one cycle of Edman degradation indicated an unblocked N-terminal Thr residue for this tryptic peptide. In contrast , our data showed a molecular protonated ion, MH + for T- la peptide at 655 mass units (mu) which is 42 mu higher than the MH ion of T-...

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Language:English
Published: University of Tehran 1992-06-01
Series:Journal of Sciences, Islamic Republic of Iran
Online Access:https://jsciences.ut.ac.ir/article_31200_331f7b41e33370ddae16190f0f100677.pdf
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description FABMS analysis of T-lb peptide before and after one cycle of Edman degradation indicated an unblocked N-terminal Thr residue for this tryptic peptide. In contrast , our data showed a molecular protonated ion, MH + for T- la peptide at 655 mass units (mu) which is 42 mu higher than the MH ion of T- 1b peptide. In addition, T- la peptide was not amenable to one cycle of manual Edman degradation. These observations suggest that the N-terminal residue of T- 1 a peptide is blocked by a chemical group having a mass of 42 mu. This observation is consistent with the presence of an N-terminal acetyl group. This prediction was further investigated by complete characterization of the gas phased fragment ions, originated from the individual peptides, using link-scanning approach. The fragment ions again suggest an acetyl group attached to an N-terminal threonine. In addition, the fragment ions provide evidence that the two peptides (T-la and T-lb) have identical structures except for the N-acetyl group
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institution DOAJ
issn 1016-1104
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language English
publishDate 1992-06-01
publisher University of Tehran
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series Journal of Sciences, Islamic Republic of Iran
spelling doaj-art-c979974309cf4a08a137ee4440aebbee2025-08-20T03:08:46ZengUniversity of TehranJournal of Sciences, Islamic Republic of Iran1016-11042345-69141992-06-013131200FAST ATOM BOMBARDMENT MASS SPECTROMETRY (FABMS) ANALYSIS OF AN N- TERMINAL - BLOCKED PEPTIDEFABMS analysis of T-lb peptide before and after one cycle of Edman degradation indicated an unblocked N-terminal Thr residue for this tryptic peptide. In contrast , our data showed a molecular protonated ion, MH + for T- la peptide at 655 mass units (mu) which is 42 mu higher than the MH ion of T- 1b peptide. In addition, T- la peptide was not amenable to one cycle of manual Edman degradation. These observations suggest that the N-terminal residue of T- 1 a peptide is blocked by a chemical group having a mass of 42 mu. This observation is consistent with the presence of an N-terminal acetyl group. This prediction was further investigated by complete characterization of the gas phased fragment ions, originated from the individual peptides, using link-scanning approach. The fragment ions again suggest an acetyl group attached to an N-terminal threonine. In addition, the fragment ions provide evidence that the two peptides (T-la and T-lb) have identical structures except for the N-acetyl grouphttps://jsciences.ut.ac.ir/article_31200_331f7b41e33370ddae16190f0f100677.pdf
spellingShingle FAST ATOM BOMBARDMENT MASS SPECTROMETRY (FABMS) ANALYSIS OF AN N- TERMINAL - BLOCKED PEPTIDE
Journal of Sciences, Islamic Republic of Iran
title FAST ATOM BOMBARDMENT MASS SPECTROMETRY (FABMS) ANALYSIS OF AN N- TERMINAL - BLOCKED PEPTIDE
title_full FAST ATOM BOMBARDMENT MASS SPECTROMETRY (FABMS) ANALYSIS OF AN N- TERMINAL - BLOCKED PEPTIDE
title_fullStr FAST ATOM BOMBARDMENT MASS SPECTROMETRY (FABMS) ANALYSIS OF AN N- TERMINAL - BLOCKED PEPTIDE
title_full_unstemmed FAST ATOM BOMBARDMENT MASS SPECTROMETRY (FABMS) ANALYSIS OF AN N- TERMINAL - BLOCKED PEPTIDE
title_short FAST ATOM BOMBARDMENT MASS SPECTROMETRY (FABMS) ANALYSIS OF AN N- TERMINAL - BLOCKED PEPTIDE
title_sort fast atom bombardment mass spectrometry fabms analysis of an n terminal blocked peptide
url https://jsciences.ut.ac.ir/article_31200_331f7b41e33370ddae16190f0f100677.pdf