Accumulated forms of thallium and cadmium inLemna minor. II. Relationship between duration of exposure and metal-protein binding

Abstract

Gel filtration chromatography (with Sephadex G25, G50 and G100) was used to separate the different forms of thallium (TI) and cadmium (Cd) in the cytosol fraction of Lemna minor and to examine the influence of the duration of metal exposure on the speciation of the two elements. A major proportion of Cd in the soluble phase was found to be bound to three groups of proteinaceous and polypeptide fractions; two of these, the high molecular weight protein fraction (Mr > 150,000) and the low polypeptide sized moieties of about Mr 1,SOO or less were constitutive entities, whereas the intermediate sized fraction (Mr 7,000-8,000) could only be detected in plants previously exposed to Cd. After 12 days of exposure to Cd this fraction accounted for the greatest part of the bound Cd in Lemna tissues. Extending the period of exposure from 18 hours to 12 days resulted in a shift in the distribution of Cd between the low and intermediate fractions. Evidence for Tl-protein binding was limited and confined to the high molecular weight fraction, and most of the Tl in the soluble phase was present in a form closely allied to the free ion. The contrasting behaviour between the two elements has been interpreted in terms of the differences in their physicochemical properties.

The Effect of Both Different Light Conditions and the pH Value on the Capacity of Salvinia minima Baker for Removing Cadmium, Lead and Chromium

“…In these experiments, it was shown that the roots were the principal accumulation site, compared to the fronds. A thorough study with the aim to investigate the distribution of cadmium between the aqueous soluble and insoluble fractions of Lemna minor [17] demonstrated that cadmium was mainly bound to the pectins and proteins in the cell wall fractions of the plant. It would appear, therefore, that the main mechanism of cadmium uptake by S. minima could also be related to the adsorption of surface pectins and proteins.…”