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. 1981 Jun;89(6):1839-45.
doi: 10.1093/oxfordjournals.jbchem.a133385.

Complete amino acid sequence of mouse liver metallothionein-II

I Y Huang, M Kimura, A Hata, H Tsunoo, A Yoshida
Free article

Complete amino acid sequence of mouse liver metallothionein-II

I Y Huang et al. J Biochem. 1981 Jun.
Free article

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.

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