DETECTION OF CROSS-LINmD PERIDES BY FAST ATOM B01WBARDMENT MASS SPECTROMETRY

The possibility of chemical modification of peptides and proteins under the condition of proteolytic digestions and FABMS analysis was investigated. The results ;indicate that among the amino acid constituents of peptides and proteins: serinefcysteine, and cystine are the most sensitive residues whi...

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Format: Article
Language:English
Published: University of Tehran 1991-12-01
Series:Journal of Sciences, Islamic Republic of Iran
Online Access:https://jsciences.ut.ac.ir/article_31441_dfc49c2611da1a6483849f5c52afa59d.pdf
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collection DOAJ
description The possibility of chemical modification of peptides and proteins under the condition of proteolytic digestions and FABMS analysis was investigated. The results ;indicate that among the amino acid constituents of peptides and proteins: serinefcysteine, and cystine are the most sensitive residues which undergo chemical modificadons under the exprimenta1 conditions. The chemical modification of these amino acids which is governed by the intrinsic properties of the peptides will result in the formation of a molecular ion mass which is 16 mu lower than the molecufitir ion of the parent peptide, MHf. Exact mass measurements of (MH-16) molecular ions indicate that these ions may cornspond to(MH-H O +H ) but not(MH-CH ) molecules. In addition, the results indicate the presence of no inter-and /or intrachain disulfide bond rearrangements uhder the experimental conditions of degradations and FABMS analyses of Lysozyme and Rihonuclease A.
format Article
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institution OA Journals
issn 1016-1104
2345-6914
language English
publishDate 1991-12-01
publisher University of Tehran
record_format Article
series Journal of Sciences, Islamic Republic of Iran
spelling doaj-art-e68421b2e1134af9b5744536fe2d56652025-08-20T02:25:51ZengUniversity of TehranJournal of Sciences, Islamic Republic of Iran1016-11042345-69141991-12-012231441DETECTION OF CROSS-LINmD PERIDES BY FAST ATOM B01WBARDMENT MASS SPECTROMETRYThe possibility of chemical modification of peptides and proteins under the condition of proteolytic digestions and FABMS analysis was investigated. The results ;indicate that among the amino acid constituents of peptides and proteins: serinefcysteine, and cystine are the most sensitive residues which undergo chemical modificadons under the exprimenta1 conditions. The chemical modification of these amino acids which is governed by the intrinsic properties of the peptides will result in the formation of a molecular ion mass which is 16 mu lower than the molecufitir ion of the parent peptide, MHf. Exact mass measurements of (MH-16) molecular ions indicate that these ions may cornspond to(MH-H O +H ) but not(MH-CH ) molecules. In addition, the results indicate the presence of no inter-and /or intrachain disulfide bond rearrangements uhder the experimental conditions of degradations and FABMS analyses of Lysozyme and Rihonuclease A.https://jsciences.ut.ac.ir/article_31441_dfc49c2611da1a6483849f5c52afa59d.pdf
spellingShingle DETECTION OF CROSS-LINmD PERIDES BY FAST ATOM B01WBARDMENT MASS SPECTROMETRY
Journal of Sciences, Islamic Republic of Iran
title DETECTION OF CROSS-LINmD PERIDES BY FAST ATOM B01WBARDMENT MASS SPECTROMETRY
title_full DETECTION OF CROSS-LINmD PERIDES BY FAST ATOM B01WBARDMENT MASS SPECTROMETRY
title_fullStr DETECTION OF CROSS-LINmD PERIDES BY FAST ATOM B01WBARDMENT MASS SPECTROMETRY
title_full_unstemmed DETECTION OF CROSS-LINmD PERIDES BY FAST ATOM B01WBARDMENT MASS SPECTROMETRY
title_short DETECTION OF CROSS-LINmD PERIDES BY FAST ATOM B01WBARDMENT MASS SPECTROMETRY
title_sort detection of cross linmd perides by fast atom b01wbardment mass spectrometry
url https://jsciences.ut.ac.ir/article_31441_dfc49c2611da1a6483849f5c52afa59d.pdf