Complete Amino Acid Sequence of Mouse Liver Metallothionein-II1
- 1 April 1981
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 89 (6) , 1839-1845
- https://doi.org/10.1093/oxfordjournals.jbchem.a133385
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-[14]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.Keywords
This publication has 5 references indexed in Scilit:
- Mouse liver metallothioneins. Purification, molecular weight, amino acid composition, and metal content.Journal of Biological Chemistry, 1978
- Mouse liver metallothioneins. Complete amino acid sequence of metallothionein-I.Journal of Biological Chemistry, 1977
- Metallothionein and its Relationship to the Metabolism of Dietary Zinc in RatsJournal of Nutrition, 1976
- RELATIVE CADMIUM-BINDING CAPACITY OF METALLOTHIONEIN AND OTHER CYTOSOLIC FRACTIONS IN VARIOUS TISSUES OF RAT1975
- Isolation and Some Properties of Human Metallothionein*Biochemistry, 1966