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Involvement of cysteine residues in the electrophoretic mobility of histone H3 in acid‐urea‐Triton gels
Author(s) -
Waterborg Jakob H.
Publication year - 1990
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150110811
Subject(s) - chemistry , cysteine , urea , moiety , residue (chemistry) , biochemistry , electrophoresis , acetic acid , histone , polyacrylamide gel electrophoresis , polyacrylamide , chromatography , polymer chemistry , stereochemistry , enzyme , gene
Carbamylation of cysteines 96 and 110 in histone H3 increases the electrophoretic mobility of this histone in acetic acid‐urea‐Triton X‐100 polyacrylamide gels but has no effect in gels lacking Triton. Residue 96 appears to be a major determinant in the affinity of histone H3 for the nonionic detergent Triton. Carbamylation and carboxymethylation of cysteine 96 caused a major loss of the gel retardation caused by Triton. Carbamylation of cysteine 110 did not affect Triton binding but prevented ionization of the thiol side‐chain moiety in the acetic acid‐urea‐Triton X‐100 gel.