Abstract
Synapsins are key phosphoproteins in the mammalian brain, and structural research on synapsins is still holding center stage. Proteins were extracted from hippocampal tissue and separated on two-dimensional gel electrophoresis (2-DE), and the spots were analyzed by MALDI-TOF-TOF and nano-LC-ESI-MS/MS. Synapsins Ia, IIa, and IIb were unambiguously identified and represented by 15 individual spots on 2-DE. Several serine phosphorylation sites were confirmed, and a novel phosphorylation site was observed at Ser-546 in synapsin IIa in all gels analyzed.
MeSH terms
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Acetylation
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Alternative Splicing
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Amino Acid Sequence
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Animals
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Electrophoresis, Gel, Two-Dimensional
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Hippocampus / chemistry*
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Male
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Methionine / chemistry
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Methylation
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Mice
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Mice, Inbred C57BL
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Molecular Sequence Data
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Nanotechnology / methods
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Phosphoproteins / chemistry*
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Phosphorylation
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Phosphoserine / analysis*
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Protein Conformation
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Protein Isoforms / chemistry
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Protein Isoforms / genetics
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Serine / chemistry*
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods
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Synapsins / chemistry*
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Synapsins / genetics
Substances
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Phosphoproteins
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Protein Isoforms
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Synapsins
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Phosphoserine
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Serine
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Methionine