The uptake behavior of rare earth elements (REEs) under pot conditions using deionized water and a REE fertilizer solution as the culture media as well as the distribution of REEs in rice proteins were studied. The uptake of REEs in rice seeds increased dramatically after a lag period of approximately three days. Roots can accumulate a much higher content of REEs than germs and the resting seeds. The REE content in each water-soluble (albumin) and salt-soluble (globulin) component of the rice seeds accounted for 5±8% and 4±6% of the total REEs, respectively. However, there are less than 1.5% of the total REEs were found in the alcohol-soluble (prolamin) and acetic acid-soluble (glutelin) components. The high performance liquid chromatography (HPLC) in the gel permeation and the reserved-phase were used to monitor changes in the molecular weight distribution changes of the soluble proteins of rice seeds during germination after having been cultured in the same solution for seven days. No changes occurred in the prolamin, while a slight change occurred in the albumin, globulin and glutelin. Fractionation of the albumin of rice seeds cultured in a REE fertilizer solution on the Sephadex G-100 column indicated that REEs, especially Ce, La, Pr and Nd, were associated mainly with biological compounds of a molecular weight between 10,000 and 12,000. Ó
Rare earth element-binding protein was isolated from maize, which was grown under greenhouse conditions and characterized in terms of molecular weight, amino acid composition, and ultraviolet absorption. The molecular weight of the maize protein was determined to be 183,000, with two distinct subunits of approximately molecular weights of 22,000 and 69,000, respectively. The protein is particularly rich in asparagine/aspartic acid, glutamine/glutamic acid, glycine, alanine, and leucine and contains 8.0% of covalently bound carbohydrate. The ultraviolet absorption of the protein is low at 280 nm and no change in the adsorption was observed with a change in pH. Compared to the unique features of the metallothioneins with a molecular weight of approximately 10,000, a high cysteine content of 30%, high absorption at 254 nm and a low absorption at 280 nm, and absorption change with pH, the REE-binding protein is unlikely to be plant metallothionein in nature. It was found that an almost twofold greater concentration was found for most of the REEs in the protein isolated from the maize with REE fertilizer use than that without REE fertilizer. This study suggests that the REE-binding protein is a glycoprotein and REEs can be firmly bound with the protein of maize roots.
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