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The primary structure of histone H3 from wheat
A M Modro1, J A Rodrigues, W F Brandt
1UCT/CSIR Research Centre for Molecular Biology, Department of Biochemistry, University of Cape Town.
Biological Chemistry Hoppe-Seyler
|March 1, 1988
Abstract:
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).