Identification of endogenous phosphorylation sites of bovine medium and low molecular weight neurofilament proteins by tandem mass spectrometry.
作者： Sarah Trimpin , April E. Mixon , Martha D. Stapels , Moo-Young Kim , Peter S. Spencer
DOI: 10.1021/BI030196Q
关键词: Tandem mass spectrometry 、 Chemistry 、 Amino acid 、 Endogeny 、 Molecular mass 、 Mass spectrometry 、 Phosphate 、 Intermediate filament 、 Phosphorylation 、 Biochemistry
摘要: Neurofilament proteins (NFP) are intermediate filaments found in the neuronal cytoskeleton. They highly phosphorylated, a condition that is believed to be responsible for assembly and stability of filaments. Matrix-assisted laser desorption/ionization (MALDI) time-of-flight (TOF) mass spectrometry (MS) shows molecular masses bovine NFP subunits 63, 105, 125 kDa NFL, NFM, NFH. Mass spectrometric de novo sequencing was used determine N-terminal sequence NFM (115 amino acids), which previously unknown. Molecular information there one-half equivalent phosphate group on NFL 24 NFM. For first time, it shown has three phosphorylation sites (Ser55, Ser66, Ser472) 22 (Ser512, Ser546, Ser554, Ser560, Thr627, Ser629, Ser634, Ser639, Thr646, Ser649, Ser654, Ser664, Ser669, Thr676, Ser679, Ser684, Ser694, Ser726, Ser750, Ser756, Ser770, Ser846) two tentative (Ser659/Thr661 Thr840). Ser...
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