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Your search keyword '"Angelika Weiler"' showing total 2 results
Start Over Author "Angelika Weiler" Topic amino acid sequence
2 results on '"Angelika Weiler"'

1. Characterization of natural peptides from bovine tissue using capillary electrophoresis, high performance liquid chromatography, matrix-assisted laser desorption ionization, and Edman degradation

Author

Angelika Weiler, Gerald Grübler, Stanka Stoeva, Rainer Lehmann, h. c. Wolfgang Voelter, and Gerd Paulus

Subjects
Molecular Sequence Data, Clinical Biochemistry, Analytical chemistry, Mass spectrometry, Biochemistry, High-performance liquid chromatography, Capillary electrophoresis–mass spectrometry, Analytical Chemistry, Organophosphorus Compounds, Capillary electrophoresis, Animals, Amino Acid Sequence, Lung, Ubiquitins, Peptide sequence, Chromatography, High Pressure Liquid, Chromatography, Edman degradation, Chemistry, Microfilament Proteins, Electrophoresis, Capillary, Thymosin, Electrophoresis, Matrix-assisted laser desorption/ionization, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Cattle, Peptides, hormones, hormone substitutes, and hormone antagonists
Abstract

A combination of high performance liquid chromatography (HPLC) and capillary electrophoresis (CE) spiking, Edman degradation, amino acid analysis and matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS) was applied for the analysis of the primary structure of beta-thymosins. CE has been used to resolve peaks which coelute on HPLC, as well as to help establish the identity of tryptic fragments in the peptide mapping experiments of the two highly homologous beta-thymosins.

Published
1996

2. Prothymosin alpha: efficient sequence determination by experimental and theoretical capillary electrophoretic support

Author

Stanka Stoeva, Wolfgang Voelter, Angelika Weiler, and Ourania E. Tsitsilonis

Subjects
Chromatography, Edman degradation, Capillary action, Chemistry, Clinical Biochemistry, Molecular Sequence Data, Protein primary structure, Analytical chemistry, Electrophoresis, Capillary, Biochemistry, Capillary electrophoresis–mass spectrometry, High-performance liquid chromatography, Analytical Chemistry, Thymosin, Electrophoresis, Capillary electrophoresis, Prothymosin α, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Animals, natural sciences, Cattle, Amino Acid Sequence, Protein Precursors, Sequence Analysis, Chromatography, High Pressure Liquid
Abstract

A rapid and efficient primary structure elucidation of prothymosin (ProT alpha) and its enzymatic fragments was performed by a combination of matrix-assisted laser desorption ionization mass spectrometry (MALDI), automatic N-terminal Edman degradation, and the available theoretical predictions of electrophoretic mobility in capillary electrophoresis (CE) as a basis suggesting active sites of ProT alpha in the different bioassays.

Published
1997

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