Other Metal-Peptide and -Protein Interactions

Other Metal-Peptide and -Protein Interactions.—The determination of protein-bound trace elements in biological material by neutron activation analysis has been described Zn, Hg, Cu, and Se were accurately detected in human liver samples, provided that most of the element concerned was protein bound. An interaction of mercury with a protein or a protein-DNA complex has been invoked to explain the partitioning of the metal in euchromatin over heterochromatin (from mouse liver nuclei) by a 10 1 ratio. Bovine retinas, isolated rod outer segments and emul-phogene extracts of rod outer segments have been shown to contain appreciable amounts of Zn , Ca and the zinc levels being light sensitive. 

The proteins induced in rat liver by copper, zinc, mercury, and silver have been identified with the previously known metallothionein induced by cadmium.  

Premakumar, and K. Rajagopalan, Arch. Biochem. Biophys., 1975,170, 242. 

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