Abstract
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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Calcitonin Gene-Related Peptide / chemistry*
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Calcium-Binding Proteins / blood
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Calcium-Binding Proteins / chemistry*
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Calcium-Binding Proteins / isolation & purification
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Cattle
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Chromatography, High Pressure Liquid
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Electrophoresis, Polyacrylamide Gel
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Humans
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Mass Spectrometry
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Molecular Sequence Data
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Nerve Tissue Proteins / chemistry*
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Neutrophils / chemistry*
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Peptide Fragments / chemistry
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S100 Proteins*
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S100A12 Protein
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Sequence Homology, Amino Acid
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Swine
Substances
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Calcium-Binding Proteins
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Nerve Tissue Proteins
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Peptide Fragments
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S100 Proteins
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S100A12 Protein
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S100A12 protein, human
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Calcitonin Gene-Related Peptide