| Literature DB >> 7287658 |
I Y Huang, M Kimura, A Hata, H Tsunoo, A Yoshida.
Abstract
The complete amino acid sequence of thionein-II, one of the two major mouse liver thionein components, was determined. The main fragmentation of thionein-II, which consists of 61 amino acid residues, was accomplished by digesting the S-[14C]-carboxymethylated protein and the cyanogen bromide-treated oxidized protein with trypsin. The peptides obtained by papain digestion of S-[14C]carboxymethylated thionein-II were used to align the major tryptic peptides. The sequence was determined by a combination of automated and manual Edman degradation techniques. Remarkable structural homology is observed in mouse thionein-I, mouse thionein-II, and thioneins from man and horse.Entities:
Mesh:
Substances:
Year: 1981 PMID: 7287658 DOI: 10.1093/oxfordjournals.jbchem.a133385
Source DB: PubMed Journal: J Biochem ISSN: 0021-924X Impact factor: 3.387