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Front Cover: Specific glutamic acid residues in targeted proteins induce exaggerated retardations in Phos‐tag SDS‐PAGE migration
Author(s) -
Kinoshita Eiji,
KinoshitaKikuta Emiko,
Karata Kiyonobu,
Kawano Toshiki,
Nishiyama Atsuhiro,
Yamato Morihisa,
Koike Tohru
Publication year - 2017
Publication title -
electrophoresis
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.201770061
Subject(s) - phos , front cover , histone , deamidation , chemistry , biochemistry , gel electrophoresis , polyacrylamide gel electrophoresis , microbiology and biotechnology , biology , cover (algebra) , dna , enzyme , mechanical engineering , engineering
Electrophoresis 2017, 38 , 1139–1146. DOI: 10.1002/elps.201600520 The front cover picture shows typical banding patterns of human histone proteins in phosphate‐affinity Phos‐tag SDS‐PAGE. Histone H2A shows extremely retarded migrations relative to the molecular weight in Phos‐tag SDS‐PAGE, despite being nonphosphorylated. In addition, Phos‐tag SDS‐PAGE permits us to detect a shift in the mobility of the phosphorylated form of histone H2A from that of the nonphosphorylated counterpart. We conclude that specific glutamic acid residues in the targeted protein induce exaggerated retardations in Phos‐tag SDS‐PAGE migration.