Abstract
Metallothioneins exhibit spectral features which have long been known to be characteristic for their mode of metal binding. In fact, studies of the absorptive and chiroptical properties of both cadmium- and zinc-containing metallothioneins of equine and human kidney have given the earliest clues that the metal ions are bound to the protein through mercaptide bonds (1,2,3). These results have since been confirmed on metallothioneins from other sources (4, 5,6) and have also been extended to their copper- (6,7), silver- (5), mercury- (5,8), and lead- (9) containing derivatives. However, there are no comparable studies on record on the solely zinc-containing forms of metallo-thionein which occur naturally in mammalian liver. The present report gives a description and tentative interpretations of the absorption and circular dichroism features of metallothionein-2 (MT-2), one of the major zinc proteins from human liver (10).
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