Labelling of non C-terminal glutamic acid during C-terminal analysis by the tritiation method when the γ-glutamyl-peptide linkage is present
When the tritiation method for C-terminal analysis is applied to glutathione the labelling of glutamic acid is evident in addition to that of the C-terminal amino acid. It is possible that glutathione, when treated with acetic anhydride in the pyridine medium, forms N-acetylglutathione. This product...
Ausführliche Beschreibung
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| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1970 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
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| Übergeordnetes Werk: |
in: Biochemical and Biophysical Research Communications - Amsterdam : Elsevier, 41(1970), 3, Seite 642-646 |
| Übergeordnetes Werk: |
volume:41 ; year:1970 ; number:3 ; pages:642-646 |
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| 245 | 1 | 0 | |a Labelling of non C-terminal glutamic acid during C-terminal analysis by the tritiation method when the γ-glutamyl-peptide linkage is present |
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| 520 | |a When the tritiation method for C-terminal analysis is applied to glutathione the labelling of glutamic acid is evident in addition to that of the C-terminal amino acid. It is possible that glutathione, when treated with acetic anhydride in the pyridine medium, forms N-acetylglutathione. This product can cyclize to form the oxazolone ring which readily incorporates tritium in the presence of ^3H"2O. The labelling of non C-terminal glutamic acid may occur in proteins or peptides due to the presence of glutathione which can form mixed disulfides with proteins or when glutamic acid is in intrachain position with the γ-glutamyl-peptide linkage because this structure is very similar to acetylglutathione. | ||
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(DE-627)NLEJ183600991 (DE-599)GBVNLZ183600991 DE-627 ger DE-627 rakwb eng Labelling of non C-terminal glutamic acid during C-terminal analysis by the tritiation method when the γ-glutamyl-peptide linkage is present 1970 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier When the tritiation method for C-terminal analysis is applied to glutathione the labelling of glutamic acid is evident in addition to that of the C-terminal amino acid. It is possible that glutathione, when treated with acetic anhydride in the pyridine medium, forms N-acetylglutathione. This product can cyclize to form the oxazolone ring which readily incorporates tritium in the presence of ^3H"2O. The labelling of non C-terminal glutamic acid may occur in proteins or peptides due to the presence of glutathione which can form mixed disulfides with proteins or when glutamic acid is in intrachain position with the γ-glutamyl-peptide linkage because this structure is very similar to acetylglutathione. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ramponi, G. oth Cappugi, G. oth Nassi, P. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 41(1970), 3, Seite 642-646 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:41 year:1970 number:3 pages:642-646 http://dx.doi.org/10.1016/0006-291X(70)90061-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 41 1970 3 642-646 |
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(DE-627)NLEJ183600991 (DE-599)GBVNLZ183600991 DE-627 ger DE-627 rakwb eng Labelling of non C-terminal glutamic acid during C-terminal analysis by the tritiation method when the γ-glutamyl-peptide linkage is present 1970 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier When the tritiation method for C-terminal analysis is applied to glutathione the labelling of glutamic acid is evident in addition to that of the C-terminal amino acid. It is possible that glutathione, when treated with acetic anhydride in the pyridine medium, forms N-acetylglutathione. This product can cyclize to form the oxazolone ring which readily incorporates tritium in the presence of ^3H"2O. The labelling of non C-terminal glutamic acid may occur in proteins or peptides due to the presence of glutathione which can form mixed disulfides with proteins or when glutamic acid is in intrachain position with the γ-glutamyl-peptide linkage because this structure is very similar to acetylglutathione. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ramponi, G. oth Cappugi, G. oth Nassi, P. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 41(1970), 3, Seite 642-646 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:41 year:1970 number:3 pages:642-646 http://dx.doi.org/10.1016/0006-291X(70)90061-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 41 1970 3 642-646 |
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(DE-627)NLEJ183600991 (DE-599)GBVNLZ183600991 DE-627 ger DE-627 rakwb eng Labelling of non C-terminal glutamic acid during C-terminal analysis by the tritiation method when the γ-glutamyl-peptide linkage is present 1970 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier When the tritiation method for C-terminal analysis is applied to glutathione the labelling of glutamic acid is evident in addition to that of the C-terminal amino acid. It is possible that glutathione, when treated with acetic anhydride in the pyridine medium, forms N-acetylglutathione. This product can cyclize to form the oxazolone ring which readily incorporates tritium in the presence of ^3H"2O. The labelling of non C-terminal glutamic acid may occur in proteins or peptides due to the presence of glutathione which can form mixed disulfides with proteins or when glutamic acid is in intrachain position with the γ-glutamyl-peptide linkage because this structure is very similar to acetylglutathione. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ramponi, G. oth Cappugi, G. oth Nassi, P. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 41(1970), 3, Seite 642-646 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:41 year:1970 number:3 pages:642-646 http://dx.doi.org/10.1016/0006-291X(70)90061-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 41 1970 3 642-646 |
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(DE-627)NLEJ183600991 (DE-599)GBVNLZ183600991 DE-627 ger DE-627 rakwb eng Labelling of non C-terminal glutamic acid during C-terminal analysis by the tritiation method when the γ-glutamyl-peptide linkage is present 1970 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier When the tritiation method for C-terminal analysis is applied to glutathione the labelling of glutamic acid is evident in addition to that of the C-terminal amino acid. It is possible that glutathione, when treated with acetic anhydride in the pyridine medium, forms N-acetylglutathione. This product can cyclize to form the oxazolone ring which readily incorporates tritium in the presence of ^3H"2O. The labelling of non C-terminal glutamic acid may occur in proteins or peptides due to the presence of glutathione which can form mixed disulfides with proteins or when glutamic acid is in intrachain position with the γ-glutamyl-peptide linkage because this structure is very similar to acetylglutathione. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ramponi, G. oth Cappugi, G. oth Nassi, P. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 41(1970), 3, Seite 642-646 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:41 year:1970 number:3 pages:642-646 http://dx.doi.org/10.1016/0006-291X(70)90061-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 41 1970 3 642-646 |
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(DE-627)NLEJ183600991 (DE-599)GBVNLZ183600991 DE-627 ger DE-627 rakwb eng Labelling of non C-terminal glutamic acid during C-terminal analysis by the tritiation method when the γ-glutamyl-peptide linkage is present 1970 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier When the tritiation method for C-terminal analysis is applied to glutathione the labelling of glutamic acid is evident in addition to that of the C-terminal amino acid. It is possible that glutathione, when treated with acetic anhydride in the pyridine medium, forms N-acetylglutathione. This product can cyclize to form the oxazolone ring which readily incorporates tritium in the presence of ^3H"2O. The labelling of non C-terminal glutamic acid may occur in proteins or peptides due to the presence of glutathione which can form mixed disulfides with proteins or when glutamic acid is in intrachain position with the γ-glutamyl-peptide linkage because this structure is very similar to acetylglutathione. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Ramponi, G. oth Cappugi, G. oth Nassi, P. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 41(1970), 3, Seite 642-646 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:41 year:1970 number:3 pages:642-646 http://dx.doi.org/10.1016/0006-291X(70)90061-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 41 1970 3 642-646 |
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Labelling of non C-terminal glutamic acid during C-terminal analysis by the tritiation method when the γ-glutamyl-peptide linkage is present |
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labelling of non c-terminal glutamic acid during c-terminal analysis by the tritiation method when the γ-glutamyl-peptide linkage is present |
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Labelling of non C-terminal glutamic acid during C-terminal analysis by the tritiation method when the γ-glutamyl-peptide linkage is present |
| abstract |
When the tritiation method for C-terminal analysis is applied to glutathione the labelling of glutamic acid is evident in addition to that of the C-terminal amino acid. It is possible that glutathione, when treated with acetic anhydride in the pyridine medium, forms N-acetylglutathione. This product can cyclize to form the oxazolone ring which readily incorporates tritium in the presence of ^3H"2O. The labelling of non C-terminal glutamic acid may occur in proteins or peptides due to the presence of glutathione which can form mixed disulfides with proteins or when glutamic acid is in intrachain position with the γ-glutamyl-peptide linkage because this structure is very similar to acetylglutathione. |
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When the tritiation method for C-terminal analysis is applied to glutathione the labelling of glutamic acid is evident in addition to that of the C-terminal amino acid. It is possible that glutathione, when treated with acetic anhydride in the pyridine medium, forms N-acetylglutathione. This product can cyclize to form the oxazolone ring which readily incorporates tritium in the presence of ^3H"2O. The labelling of non C-terminal glutamic acid may occur in proteins or peptides due to the presence of glutathione which can form mixed disulfides with proteins or when glutamic acid is in intrachain position with the γ-glutamyl-peptide linkage because this structure is very similar to acetylglutathione. |
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When the tritiation method for C-terminal analysis is applied to glutathione the labelling of glutamic acid is evident in addition to that of the C-terminal amino acid. It is possible that glutathione, when treated with acetic anhydride in the pyridine medium, forms N-acetylglutathione. This product can cyclize to form the oxazolone ring which readily incorporates tritium in the presence of ^3H"2O. The labelling of non C-terminal glutamic acid may occur in proteins or peptides due to the presence of glutathione which can form mixed disulfides with proteins or when glutamic acid is in intrachain position with the γ-glutamyl-peptide linkage because this structure is very similar to acetylglutathione. |
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