Amino Acid Sequence Determination of Human S100A12 (P6, Calgranulin C, CGRP, CAAF1) by Tandem Mass Spectrometry

S100A12 has been isolated from human neutrophils. The molecular weight and the amino acid sequence of S100A12 was determined by electrospray-mass spectrometry, tandem mass spectrometry and Edman microsequence analysis. Interestingly, a sequence comparison of S100A12 with all known human S100 protein...

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Veröffentlicht in:	Biochemical and biophysical research communications 1996-08, Vol.225 (1), p.146-150
Hauptverfasser:	Ilg, Evelyn C., Troxler, Heinz, Bürgisser, Daniel M., Kuster, Thomas, Markert, Michèle, Guignard, Florence, Hunziker, Peter, Birchler, Neil, Heizmann, Claus W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Calcitonin Gene-Related Peptide - chemistry Calcium-Binding Proteins - blood Calcium-Binding Proteins - chemistry Calcium-Binding Proteins - isolation & purification Cattle Chromatography, High Pressure Liquid Electrophoresis, Polyacrylamide Gel Humans Mass Spectrometry Molecular Sequence Data Nerve Tissue Proteins - chemistry Neutrophils - chemistry Peptide Fragments - chemistry S100 Proteins S100A12 Protein Sequence Homology, Amino Acid Swine
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Zusammenfassung:	S100A12 has been isolated from human neutrophils. The molecular weight and the amino acid sequence of S100A12 was determined by electrospray-mass spectrometry, tandem mass spectrometry and Edman microsequence analysis. Interestingly, a sequence comparison of S100A12 with all known human S100 proteins revealed that S100A12 is the most divergent of the S100 proteins.
ISSN:	0006-291X 1090-2104
DOI:	10.1006/bbrc.1996.1144