The primary structure of histone H3 from wheat.
Wheat embryo histone H3 has been isolated and purified and the elucidation of the complete amino-acid sequence is described. Peptides were generated by cleavages with CNBr, S. aureus V8 proteinase, endoproteinase Lys-C and trypsin. The peptides were purified by HPLC and the sequence determined by solid-state and gas-phase sequencing methodology. The amino-acid sequence of the protein is identical to pea embryo histone H3 and the sequence deduced from the nucleotide sequence of a wheat embryo histone gene (Tabata T. et al. (1984) Mol. Gen. Genet. 196, 397-400).
Modro
A M
AM
UCT/CSIR Research Centre for Molecular Biology, Department of Biochemistry, University of Cape Town.
Rodrigues
J A
JA
Brandt
W F
WF
von Holt
C
C
D000595:Amino Acid Sequence; D006657:Histones / Q000302:isolation & purification; D007202:Indicators and Reagents; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases; D010944:Plants / Q000032:analysis*; D014908:Triticum / Q000032:analysis
D006657:Histones; D007202:Indicators and Reagents; D010446:Peptide Fragments; D010447:Peptide Hydrolases