An active-site peptide from human triose phosphate isomerase
Chloroacetol phosphate totally inactivates human triose phosphate isomerase by the selective modification of a single residue per catalytic subunit. The stability of the protein-reagent bond and the analogies of this active-site modification to those described previously for isomerases from other sp...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1973 |
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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, 52(1973), 2, Seite 388-393 |
| Übergeordnetes Werk: |
volume:52 ; year:1973 ; number:2 ; pages:388-393 |
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| 520 | |a Chloroacetol phosphate totally inactivates human triose phosphate isomerase by the selective modification of a single residue per catalytic subunit. The stability of the protein-reagent bond and the analogies of this active-site modification to those described previously for isomerases from other species indicate that inactivation results from the esterification of an essential glutamyl γ-carboxylate. From peptide maps and their autoradiograms, we conclude that the primary structure adjacent to the glutamyl residue is the same as or similar to that found in triose phosphate isomerases from rabbit and chicken muscle and from yeast. | ||
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(DE-627)NLEJ18358967X (DE-599)GBVNLZ18358967X DE-627 ger DE-627 rakwb eng An active-site peptide from human triose phosphate isomerase 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Chloroacetol phosphate totally inactivates human triose phosphate isomerase by the selective modification of a single residue per catalytic subunit. The stability of the protein-reagent bond and the analogies of this active-site modification to those described previously for isomerases from other species indicate that inactivation results from the esterification of an essential glutamyl γ-carboxylate. From peptide maps and their autoradiograms, we conclude that the primary structure adjacent to the glutamyl residue is the same as or similar to that found in triose phosphate isomerases from rabbit and chicken muscle and from yeast. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hartman, F.C. oth Gracy, R.W. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 52(1973), 2, Seite 388-393 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:52 year:1973 number:2 pages:388-393 http://dx.doi.org/10.1016/0006-291X(73)90723-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 52 1973 2 388-393 |
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(DE-627)NLEJ18358967X (DE-599)GBVNLZ18358967X DE-627 ger DE-627 rakwb eng An active-site peptide from human triose phosphate isomerase 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Chloroacetol phosphate totally inactivates human triose phosphate isomerase by the selective modification of a single residue per catalytic subunit. The stability of the protein-reagent bond and the analogies of this active-site modification to those described previously for isomerases from other species indicate that inactivation results from the esterification of an essential glutamyl γ-carboxylate. From peptide maps and their autoradiograms, we conclude that the primary structure adjacent to the glutamyl residue is the same as or similar to that found in triose phosphate isomerases from rabbit and chicken muscle and from yeast. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hartman, F.C. oth Gracy, R.W. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 52(1973), 2, Seite 388-393 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:52 year:1973 number:2 pages:388-393 http://dx.doi.org/10.1016/0006-291X(73)90723-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 52 1973 2 388-393 |
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(DE-627)NLEJ18358967X (DE-599)GBVNLZ18358967X DE-627 ger DE-627 rakwb eng An active-site peptide from human triose phosphate isomerase 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Chloroacetol phosphate totally inactivates human triose phosphate isomerase by the selective modification of a single residue per catalytic subunit. The stability of the protein-reagent bond and the analogies of this active-site modification to those described previously for isomerases from other species indicate that inactivation results from the esterification of an essential glutamyl γ-carboxylate. From peptide maps and their autoradiograms, we conclude that the primary structure adjacent to the glutamyl residue is the same as or similar to that found in triose phosphate isomerases from rabbit and chicken muscle and from yeast. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hartman, F.C. oth Gracy, R.W. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 52(1973), 2, Seite 388-393 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:52 year:1973 number:2 pages:388-393 http://dx.doi.org/10.1016/0006-291X(73)90723-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 52 1973 2 388-393 |
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(DE-627)NLEJ18358967X (DE-599)GBVNLZ18358967X DE-627 ger DE-627 rakwb eng An active-site peptide from human triose phosphate isomerase 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Chloroacetol phosphate totally inactivates human triose phosphate isomerase by the selective modification of a single residue per catalytic subunit. The stability of the protein-reagent bond and the analogies of this active-site modification to those described previously for isomerases from other species indicate that inactivation results from the esterification of an essential glutamyl γ-carboxylate. From peptide maps and their autoradiograms, we conclude that the primary structure adjacent to the glutamyl residue is the same as or similar to that found in triose phosphate isomerases from rabbit and chicken muscle and from yeast. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hartman, F.C. oth Gracy, R.W. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 52(1973), 2, Seite 388-393 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:52 year:1973 number:2 pages:388-393 http://dx.doi.org/10.1016/0006-291X(73)90723-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 52 1973 2 388-393 |
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(DE-627)NLEJ18358967X (DE-599)GBVNLZ18358967X DE-627 ger DE-627 rakwb eng An active-site peptide from human triose phosphate isomerase 1973 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Chloroacetol phosphate totally inactivates human triose phosphate isomerase by the selective modification of a single residue per catalytic subunit. The stability of the protein-reagent bond and the analogies of this active-site modification to those described previously for isomerases from other species indicate that inactivation results from the esterification of an essential glutamyl γ-carboxylate. From peptide maps and their autoradiograms, we conclude that the primary structure adjacent to the glutamyl residue is the same as or similar to that found in triose phosphate isomerases from rabbit and chicken muscle and from yeast. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Hartman, F.C. oth Gracy, R.W. oth in Biochemical and Biophysical Research Communications Amsterdam : Elsevier 52(1973), 2, Seite 388-393 (DE-627)NLEJ176855645 (DE-600)1461396-7 0006-291X nnns volume:52 year:1973 number:2 pages:388-393 http://dx.doi.org/10.1016/0006-291X(73)90723-7 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 52 1973 2 388-393 |
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An active-site peptide from human triose phosphate isomerase |
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Chloroacetol phosphate totally inactivates human triose phosphate isomerase by the selective modification of a single residue per catalytic subunit. The stability of the protein-reagent bond and the analogies of this active-site modification to those described previously for isomerases from other species indicate that inactivation results from the esterification of an essential glutamyl γ-carboxylate. From peptide maps and their autoradiograms, we conclude that the primary structure adjacent to the glutamyl residue is the same as or similar to that found in triose phosphate isomerases from rabbit and chicken muscle and from yeast. |
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Chloroacetol phosphate totally inactivates human triose phosphate isomerase by the selective modification of a single residue per catalytic subunit. The stability of the protein-reagent bond and the analogies of this active-site modification to those described previously for isomerases from other species indicate that inactivation results from the esterification of an essential glutamyl γ-carboxylate. From peptide maps and their autoradiograms, we conclude that the primary structure adjacent to the glutamyl residue is the same as or similar to that found in triose phosphate isomerases from rabbit and chicken muscle and from yeast. |
| abstract_unstemmed |
Chloroacetol phosphate totally inactivates human triose phosphate isomerase by the selective modification of a single residue per catalytic subunit. The stability of the protein-reagent bond and the analogies of this active-site modification to those described previously for isomerases from other species indicate that inactivation results from the esterification of an essential glutamyl γ-carboxylate. From peptide maps and their autoradiograms, we conclude that the primary structure adjacent to the glutamyl residue is the same as or similar to that found in triose phosphate isomerases from rabbit and chicken muscle and from yeast. |
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An active-site peptide from human triose phosphate isomerase |
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