Isolation and enzymatic fragmentation of the coeliac-active gliadin peptide CT-1

Summary Investigations on the structure/toxicity relationships of gliadin peptides were continued with the coeliac-active gliadin peptide CT-1, which is derived from the N-terminal portion (residues 3–24 of the amino acid sequence) ofα-gliadins [this journal (1986) 182:115–117]. CT-1 was produced by...
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Gespeichert in:

Autor*in:	Wieser, Herbert [verfasserIn] Belitz, Hans-Dieter

Format:	Artikel
Sprache:	Englisch

Erschienen:	1992

Schlagwörter:	Enzyme Peptide HPLC Amino Acid Sequence Toxic Effect

Anmerkung:	© Springer-Verlag 1992

Übergeordnetes Werk:	Enthalten in: Zeitschrift für Lebensmittel-Untersuchung und -Forschung - Springer-Verlag, 1943, 195(1992), 1 vom: Juli, Seite 22-26
Übergeordnetes Werk:	volume:195 ; year:1992 ; number:1 ; month:07 ; pages:22-26

Links:	Volltext

DOI / URN:	10.1007/BF01197834

Katalog-ID:	OLC2029941778

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520			\|a Summary Investigations on the structure/toxicity relationships of gliadin peptides were continued with the coeliac-active gliadin peptide CT-1, which is derived from the N-terminal portion (residues 3–24 of the amino acid sequence) ofα-gliadins [this journal (1986) 182:115–117]. CT-1 was produced by chymotryptic digestion and reversed-phase (RP) HPLC from the peptide fraction G3 [this journal (1992) 194:1–6] and digested with the proteases endoproteinase Glu-C, pancreatin, papain and thermolysin. The fragment peptids were separated by preparative RP-HPLC and characterized by amino acid analysis. On the basis of the specifity of the enzymes for CT-1 and the toxic effect of enzymatic hydrolysates of gliadin described in the literature, the significance of partial sequences, in particular of the sequence -Pro-Ser-Gln-Gln-Gln-Pro- for the coeliac-toxicity effect, is discussed.
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allfields	10.1007/BF01197834 doi (DE-627)OLC2029941778 (DE-He213)BF01197834-p DE-627 ger DE-627 rakwb eng 630 640 VZ Wieser, Herbert verfasserin aut Isolation and enzymatic fragmentation of the coeliac-active gliadin peptide CT-1 1992 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1992 Summary Investigations on the structure/toxicity relationships of gliadin peptides were continued with the coeliac-active gliadin peptide CT-1, which is derived from the N-terminal portion (residues 3–24 of the amino acid sequence) ofα-gliadins [this journal (1986) 182:115–117]. CT-1 was produced by chymotryptic digestion and reversed-phase (RP) HPLC from the peptide fraction G3 [this journal (1992) 194:1–6] and digested with the proteases endoproteinase Glu-C, pancreatin, papain and thermolysin. The fragment peptids were separated by preparative RP-HPLC and characterized by amino acid analysis. On the basis of the specifity of the enzymes for CT-1 and the toxic effect of enzymatic hydrolysates of gliadin described in the literature, the significance of partial sequences, in particular of the sequence -Pro-Ser-Gln-Gln-Gln-Pro- for the coeliac-toxicity effect, is discussed. Enzyme Peptide HPLC Amino Acid Sequence Toxic Effect Belitz, Hans-Dieter aut Enthalten in Zeitschrift für Lebensmittel-Untersuchung und -Forschung Springer-Verlag, 1943 195(1992), 1 vom: Juli, Seite 22-26 (DE-627)12947407X (DE-600)203000-7 (DE-576)01485192X 0044-3026 nnns volume:195 year:1992 number:1 month:07 pages:22-26 https://doi.org/10.1007/BF01197834 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_183 GBV_ILN_252 GBV_ILN_2004 GBV_ILN_2006 GBV_ILN_2010 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4027 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4219 GBV_ILN_4247 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4319 GBV_ILN_4328 AR 195 1992 1 07 22-26
spelling	10.1007/BF01197834 doi (DE-627)OLC2029941778 (DE-He213)BF01197834-p DE-627 ger DE-627 rakwb eng 630 640 VZ Wieser, Herbert verfasserin aut Isolation and enzymatic fragmentation of the coeliac-active gliadin peptide CT-1 1992 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1992 Summary Investigations on the structure/toxicity relationships of gliadin peptides were continued with the coeliac-active gliadin peptide CT-1, which is derived from the N-terminal portion (residues 3–24 of the amino acid sequence) ofα-gliadins [this journal (1986) 182:115–117]. CT-1 was produced by chymotryptic digestion and reversed-phase (RP) HPLC from the peptide fraction G3 [this journal (1992) 194:1–6] and digested with the proteases endoproteinase Glu-C, pancreatin, papain and thermolysin. The fragment peptids were separated by preparative RP-HPLC and characterized by amino acid analysis. On the basis of the specifity of the enzymes for CT-1 and the toxic effect of enzymatic hydrolysates of gliadin described in the literature, the significance of partial sequences, in particular of the sequence -Pro-Ser-Gln-Gln-Gln-Pro- for the coeliac-toxicity effect, is discussed. Enzyme Peptide HPLC Amino Acid Sequence Toxic Effect Belitz, Hans-Dieter aut Enthalten in Zeitschrift für Lebensmittel-Untersuchung und -Forschung Springer-Verlag, 1943 195(1992), 1 vom: Juli, Seite 22-26 (DE-627)12947407X (DE-600)203000-7 (DE-576)01485192X 0044-3026 nnns volume:195 year:1992 number:1 month:07 pages:22-26 https://doi.org/10.1007/BF01197834 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_183 GBV_ILN_252 GBV_ILN_2004 GBV_ILN_2006 GBV_ILN_2010 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4027 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4219 GBV_ILN_4247 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4319 GBV_ILN_4328 AR 195 1992 1 07 22-26
allfields_unstemmed	10.1007/BF01197834 doi (DE-627)OLC2029941778 (DE-He213)BF01197834-p DE-627 ger DE-627 rakwb eng 630 640 VZ Wieser, Herbert verfasserin aut Isolation and enzymatic fragmentation of the coeliac-active gliadin peptide CT-1 1992 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1992 Summary Investigations on the structure/toxicity relationships of gliadin peptides were continued with the coeliac-active gliadin peptide CT-1, which is derived from the N-terminal portion (residues 3–24 of the amino acid sequence) ofα-gliadins [this journal (1986) 182:115–117]. CT-1 was produced by chymotryptic digestion and reversed-phase (RP) HPLC from the peptide fraction G3 [this journal (1992) 194:1–6] and digested with the proteases endoproteinase Glu-C, pancreatin, papain and thermolysin. The fragment peptids were separated by preparative RP-HPLC and characterized by amino acid analysis. On the basis of the specifity of the enzymes for CT-1 and the toxic effect of enzymatic hydrolysates of gliadin described in the literature, the significance of partial sequences, in particular of the sequence -Pro-Ser-Gln-Gln-Gln-Pro- for the coeliac-toxicity effect, is discussed. Enzyme Peptide HPLC Amino Acid Sequence Toxic Effect Belitz, Hans-Dieter aut Enthalten in Zeitschrift für Lebensmittel-Untersuchung und -Forschung Springer-Verlag, 1943 195(1992), 1 vom: Juli, Seite 22-26 (DE-627)12947407X (DE-600)203000-7 (DE-576)01485192X 0044-3026 nnns volume:195 year:1992 number:1 month:07 pages:22-26 https://doi.org/10.1007/BF01197834 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_183 GBV_ILN_252 GBV_ILN_2004 GBV_ILN_2006 GBV_ILN_2010 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4027 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4219 GBV_ILN_4247 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4319 GBV_ILN_4328 AR 195 1992 1 07 22-26
allfieldsGer	10.1007/BF01197834 doi (DE-627)OLC2029941778 (DE-He213)BF01197834-p DE-627 ger DE-627 rakwb eng 630 640 VZ Wieser, Herbert verfasserin aut Isolation and enzymatic fragmentation of the coeliac-active gliadin peptide CT-1 1992 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1992 Summary Investigations on the structure/toxicity relationships of gliadin peptides were continued with the coeliac-active gliadin peptide CT-1, which is derived from the N-terminal portion (residues 3–24 of the amino acid sequence) ofα-gliadins [this journal (1986) 182:115–117]. CT-1 was produced by chymotryptic digestion and reversed-phase (RP) HPLC from the peptide fraction G3 [this journal (1992) 194:1–6] and digested with the proteases endoproteinase Glu-C, pancreatin, papain and thermolysin. The fragment peptids were separated by preparative RP-HPLC and characterized by amino acid analysis. On the basis of the specifity of the enzymes for CT-1 and the toxic effect of enzymatic hydrolysates of gliadin described in the literature, the significance of partial sequences, in particular of the sequence -Pro-Ser-Gln-Gln-Gln-Pro- for the coeliac-toxicity effect, is discussed. Enzyme Peptide HPLC Amino Acid Sequence Toxic Effect Belitz, Hans-Dieter aut Enthalten in Zeitschrift für Lebensmittel-Untersuchung und -Forschung Springer-Verlag, 1943 195(1992), 1 vom: Juli, Seite 22-26 (DE-627)12947407X (DE-600)203000-7 (DE-576)01485192X 0044-3026 nnns volume:195 year:1992 number:1 month:07 pages:22-26 https://doi.org/10.1007/BF01197834 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_183 GBV_ILN_252 GBV_ILN_2004 GBV_ILN_2006 GBV_ILN_2010 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4027 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4219 GBV_ILN_4247 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4319 GBV_ILN_4328 AR 195 1992 1 07 22-26
allfieldsSound	10.1007/BF01197834 doi (DE-627)OLC2029941778 (DE-He213)BF01197834-p DE-627 ger DE-627 rakwb eng 630 640 VZ Wieser, Herbert verfasserin aut Isolation and enzymatic fragmentation of the coeliac-active gliadin peptide CT-1 1992 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer-Verlag 1992 Summary Investigations on the structure/toxicity relationships of gliadin peptides were continued with the coeliac-active gliadin peptide CT-1, which is derived from the N-terminal portion (residues 3–24 of the amino acid sequence) ofα-gliadins [this journal (1986) 182:115–117]. CT-1 was produced by chymotryptic digestion and reversed-phase (RP) HPLC from the peptide fraction G3 [this journal (1992) 194:1–6] and digested with the proteases endoproteinase Glu-C, pancreatin, papain and thermolysin. The fragment peptids were separated by preparative RP-HPLC and characterized by amino acid analysis. On the basis of the specifity of the enzymes for CT-1 and the toxic effect of enzymatic hydrolysates of gliadin described in the literature, the significance of partial sequences, in particular of the sequence -Pro-Ser-Gln-Gln-Gln-Pro- for the coeliac-toxicity effect, is discussed. Enzyme Peptide HPLC Amino Acid Sequence Toxic Effect Belitz, Hans-Dieter aut Enthalten in Zeitschrift für Lebensmittel-Untersuchung und -Forschung Springer-Verlag, 1943 195(1992), 1 vom: Juli, Seite 22-26 (DE-627)12947407X (DE-600)203000-7 (DE-576)01485192X 0044-3026 nnns volume:195 year:1992 number:1 month:07 pages:22-26 https://doi.org/10.1007/BF01197834 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-CHE SSG-OPC-FOR GBV_ILN_11 GBV_ILN_20 GBV_ILN_21 GBV_ILN_22 GBV_ILN_23 GBV_ILN_31 GBV_ILN_40 GBV_ILN_62 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_183 GBV_ILN_252 GBV_ILN_2004 GBV_ILN_2006 GBV_ILN_2010 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2360 GBV_ILN_4012 GBV_ILN_4027 GBV_ILN_4035 GBV_ILN_4036 GBV_ILN_4046 GBV_ILN_4219 GBV_ILN_4247 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4310 GBV_ILN_4319 GBV_ILN_4328 AR 195 1992 1 07 22-26
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topic_facet	Enzyme Peptide HPLC Amino Acid Sequence Toxic Effect
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author	Wieser, Herbert
spellingShingle	Wieser, Herbert ddc 630 misc Enzyme misc Peptide misc HPLC misc Amino Acid Sequence misc Toxic Effect Isolation and enzymatic fragmentation of the coeliac-active gliadin peptide CT-1
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topic_title	630 640 VZ Isolation and enzymatic fragmentation of the coeliac-active gliadin peptide CT-1 Enzyme Peptide HPLC Amino Acid Sequence Toxic Effect
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title	Isolation and enzymatic fragmentation of the coeliac-active gliadin peptide CT-1
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title_full	Isolation and enzymatic fragmentation of the coeliac-active gliadin peptide CT-1
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title_sort	isolation and enzymatic fragmentation of the coeliac-active gliadin peptide ct-1
title_auth	Isolation and enzymatic fragmentation of the coeliac-active gliadin peptide CT-1
abstract	Summary Investigations on the structure/toxicity relationships of gliadin peptides were continued with the coeliac-active gliadin peptide CT-1, which is derived from the N-terminal portion (residues 3–24 of the amino acid sequence) ofα-gliadins [this journal (1986) 182:115–117]. CT-1 was produced by chymotryptic digestion and reversed-phase (RP) HPLC from the peptide fraction G3 [this journal (1992) 194:1–6] and digested with the proteases endoproteinase Glu-C, pancreatin, papain and thermolysin. The fragment peptids were separated by preparative RP-HPLC and characterized by amino acid analysis. On the basis of the specifity of the enzymes for CT-1 and the toxic effect of enzymatic hydrolysates of gliadin described in the literature, the significance of partial sequences, in particular of the sequence -Pro-Ser-Gln-Gln-Gln-Pro- for the coeliac-toxicity effect, is discussed. © Springer-Verlag 1992
abstractGer	Summary Investigations on the structure/toxicity relationships of gliadin peptides were continued with the coeliac-active gliadin peptide CT-1, which is derived from the N-terminal portion (residues 3–24 of the amino acid sequence) ofα-gliadins [this journal (1986) 182:115–117]. CT-1 was produced by chymotryptic digestion and reversed-phase (RP) HPLC from the peptide fraction G3 [this journal (1992) 194:1–6] and digested with the proteases endoproteinase Glu-C, pancreatin, papain and thermolysin. The fragment peptids were separated by preparative RP-HPLC and characterized by amino acid analysis. On the basis of the specifity of the enzymes for CT-1 and the toxic effect of enzymatic hydrolysates of gliadin described in the literature, the significance of partial sequences, in particular of the sequence -Pro-Ser-Gln-Gln-Gln-Pro- for the coeliac-toxicity effect, is discussed. © Springer-Verlag 1992
abstract_unstemmed	Summary Investigations on the structure/toxicity relationships of gliadin peptides were continued with the coeliac-active gliadin peptide CT-1, which is derived from the N-terminal portion (residues 3–24 of the amino acid sequence) ofα-gliadins [this journal (1986) 182:115–117]. CT-1 was produced by chymotryptic digestion and reversed-phase (RP) HPLC from the peptide fraction G3 [this journal (1992) 194:1–6] and digested with the proteases endoproteinase Glu-C, pancreatin, papain and thermolysin. The fragment peptids were separated by preparative RP-HPLC and characterized by amino acid analysis. On the basis of the specifity of the enzymes for CT-1 and the toxic effect of enzymatic hydrolysates of gliadin described in the literature, the significance of partial sequences, in particular of the sequence -Pro-Ser-Gln-Gln-Gln-Pro- for the coeliac-toxicity effect, is discussed. © Springer-Verlag 1992
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title_short	Isolation and enzymatic fragmentation of the coeliac-active gliadin peptide CT-1
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