title: The primary structure of the histone H2A(2) type from wheat germ. A core histone type with both, N-terminal and C-terminal extensions.
abstract: The histone H2A(2) type from wheat germ comprises at least two highly homologous isohistones with 151 amino acid residues. Microheterogeneity occurs mainly at the N-terminal and C-terminal regions. These isohistones have both N-terminal (7 amino acid residues) and C-terminal (15 amino acid residues) extensions relative to calf thymus histone H2A.
authors: Department of Biochemistry, University of Cape Town, Rondebosch, South Africa.
authors: J
authors: J
authors: de Andrade Rodrigues
authors: W F
authors: WF
authors: Brandt
authors: C
authors: C
authors: Von Holt
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002852:Chromatography, Ion Exchange; D006657:Histones / Q000032:analysis* / Q000235:genetics; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D013950:Thymus Gland; D014908:Triticum / Q000032:analysis* / Q000235:genetics
chemical_list: D000596:Amino Acids; D006657:Histones; D010446:Peptide Fragments