© Bestenbalt
2002-2007
Reference [1]
[1] Hunziker PE, Kaur P, Wan M, Kanzig A. (1995), Biochem. J. 306, 265-270. Primary structures of 7 metallothioneins from rabbit tissue
Abstract. Metallothionein from tissues of rabbits exposed to
cadmium chloride was separated into seven distinct isoforms by reverse-phase
liquid chromatography and their complete amino acid sequences were determined.
Five of the seven isometallothioneins showed structural features so far not
identified in other mammalian metallothioneins. Thus, two isoproteins contain a
polypeptide with a chain length of 62 rather than 61 amino acid residues. Two
isoforms are characterized by an additional positive charge and one by the
presence of an isopeptide bond between aspartic acid and serine in the
N-terminal half of the protein. The isoproteins characterized were identified
from different sources: rabbit liver and kidney and a rabbit kidney cell-line
(RK-13). In all three, the structural characteristics of the individual isoforms
are retained, indicating that in the different tissues the same mechanisms
control the synthesis and the stability of the different cadmium-induced isoMTs.
PMID: 7864820