Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 1 de 1
Filter
Add more filters










Database
Language
Publication year range
1.
Biol Chem Hoppe Seyler ; 369(3): 193-7, 1988 Mar.
Article in English | MEDLINE | ID: mdl-3285855

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).


Subject(s)
Histones , Plants/analysis , Amino Acid Sequence , Histones/isolation & purification , Indicators and Reagents , Molecular Sequence Data , Peptide Fragments/analysis , Peptide Hydrolases , Triticum/analysis
SELECTION OF CITATIONS
SEARCH DETAIL
...