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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Published inBiochemical and biophysical research communications Vol. 225; no. 1; pp. 146 - 150
Main Authors Ilg, Evelyn C., Troxler, Heinz, Bürgisser, Daniel M., Kuster, Thomas, Markert, Michèle, Guignard, Florence, Hunziker, Peter, Birchler, Neil, Heizmann, Claus W.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 05.08.1996
Subjects
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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Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1996.1144