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Comparative study of tobacco Cd-binding peptide and rat liver metallothionein: structures and metal binding properties

Conference · · Plant Physiol., Suppl.; (United States)
OSTI ID:5233213
Comparison of amino acid composition and sequence of tobacco Cd-binding peptide from leaves of plants grown in 3 or 90..mu..M Cd and cultured cells (90..mu..M Cd) with that of rat liver metallothionein (MT) demonstrate the unrelatedness of these molecules. Differences in structure are further shown by the lack of cross reactivity between the Cd-peptide and antibodies raised against MT. Studies of the effects of pII and salt (GuHCl) on Cd binding indicate that MT binds the metal with a higher affinity than does tobacco Cd-peptide (50% dissociation at pH 3.5 and 5.0, respectively). Suspension-cultured tobacco cells were grown in the presence of /sup 35/S and 90..mu..M Cd, 90..mu..M Cd+150..mu..M Zn or 150..mu..M Zn and labeled ligand (/sup 35/S) was only formed when Cd was present. Efforts to demonstrate Zn binding to ligand of Cd-peptide in vitro were unsuccessful. Studies of Cu inducibility and binding to ligand are in progress. MT is inducible by Cu, Zn, Cd and other heavy metal and a number of the proposed functions of this protein in animals involve Cu and Zn binding. The question of Zn and Cu binding to plant Cd-peptides is crucial to understanding the function(s) of these Cd-inducible, Cd-accumulating forms.
Research Organization:
Univ. of Kentucky, Lexington
OSTI ID:
5233213
Conference Information:
Journal Name: Plant Physiol., Suppl.; (United States) Journal Volume: 80:4
Country of Publication:
United States
Language:
English