BernheimV1, Main, Exploration, bibRecord, 000952

Combination of high-performance anion-exchange chromatography and electrospray mass spectrometry for analysis of the in vitro O-glycosylated mucin motif peptide

Identifieur interne : 000952 ( Main/Exploration ); précédent : 000951; suivant : 000953

Combination of high-performance anion-exchange chromatography and electrospray mass spectrometry for analysis of the in vitro O-glycosylated mucin motif peptide

Auteurs : Daniel Tetaert [France] ; Benoît Soudan [France] ; Jean-Marc Lo-Guidice [France] ; Colette Richet [France] ; Pierre Degand [France] ; Guy Boussard [France] ; Christophe Mariller [France] ; Geneviève Spik [France]

Source :

Journal of Chromatography B: Biomedical Sciences and Applications [ 0378-4347 ] ; 1994.

RBID : ISTEX:1E13CD5136E74B98A1142997B01FE799DA931485

English descriptors

Teeft :
- Alanine residues, Amperometric detection, Beckman ultrasphere, Biochem, Biol, Chem, Chromatogr, Colon, Dionex system, Electrospray mass spectrometry, Galnac, Galnac residues, Galnac transferase, Galnac transferases, Glycopeptides, Glycosylated products, Gradient elution, Homogenate, Hpaec, Hplc, Human stomach, Hydroxyamino, Hydroxyamino acids, Isocratic elution, Mass spectra, Microsomal homogenates, Microsomal preparations, Microsome preparation, Peaks fractions, Peptide, Peptide ttsaptts, Pore size, Reaction products, Sodium acetate, Synthetic peptide substrate, Tetaert, Threonine residues, Transferase.

Abstract

Abstract: Reversed-phase high-performance liquid chromatography (HPLC) and high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection were developed for the study of products obtained from the in vitro O-glycosylation of a mucin motif peptide, TTSAPTTS, the most representative sequence encoded by the human gene MUC5C. After incubation of the peptide, which is rich in clustered hydroxyamino acids, by both human colonic and gastric microsomal homogenates, the glycosylated products were separated by HPLC and HPAEC and analysed by electrospray mass spectrometry (ES-MS). The combination of HPAEC and ES-MS was the approach used for evaluating the differences between the polypeptide N-acetylgalactosaminyltransferase activity in different digestive tissues.

Url:

https://api.istex.fr/document/1E13CD5136E74B98A1142997B01FE799DA931485/fulltext/pdf

DOI: 10.1016/0378-4347(94)00223-1

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<front><div type="abstract" xml:lang="en">Abstract: Reversed-phase high-performance liquid chromatography (HPLC) and high-performance anion-exchange chromatography (HPAEC) with pulsed amperometric detection were developed for the study of products obtained from the in vitro O-glycosylation of a mucin motif peptide, TTSAPTTS, the most representative sequence encoded by the human gene MUC5C. After incubation of the peptide, which is rich in clustered hydroxyamino acids, by both human colonic and gastric microsomal homogenates, the glycosylated products were separated by HPLC and HPAEC and analysed by electrospray mass spectrometry (ES-MS). The combination of HPAEC and ES-MS was the approach used for evaluating the differences between the polypeptide N-acetylgalactosaminyltransferase activity in different digestive tissues.</div>
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Combination of high-performance anion-exchange chromatography and electrospray mass spectrometry for analysis of the in vitro O-glycosylated mucin motif peptide

Combination of high-performance anion-exchange chromatography and electrospray mass spectrometry for analysis of the in vitro O-glycosylated mucin motif peptide

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri