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- W2008595952 abstract "A Cd-binding protein was isolated from pea plants (Pisum sativum L. c.v. Wunder von Kelvedon) grown in the presence of 0.5 mg Cd/1 nutrient solution. After Sephadex G-75 gel filtration of a Cd-containing leaf homogenate a high proportion of the metal was found in the 6,000–10,000 molecular weight fraction, which coincided with a 280/250 nm absorption ratio of < 1.0. DEAE-cellulose chromatography of the 6,000–10,000 molecular weight fraction resulted in one Cd-containing peak, which eluted at 0.67 M Tris/HCl and showed a low 280/250 nm absorption ratio. The ultraviolett absorption spectrum and its changes with pH, respectively, of this protein fraction were characteristic of metallothionein. Concomitant purification of a Cd-containing rat liver homogenate under nearly identical conditions resulted in two metallothioneins, MT-A and MT-B eluting from the DEAE-cellulose at 0.08–0.12 M Tris/ HCl. The metal contents (µg Cd/mg protein) of the proteins were 8.6 (pea plant) and 8.07 and 8.23 (MT-A and MT-B), respectively. Immunological comparison by Ouchterlony double diffusion did not reveal any cross-reactivity between the purified plant protein and antisera to the rat liver metallothioneins MT-A and MT-B. The properties of the Cd-binding protein from Pisum sativum are discussed." @default.
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- W2008595952 title "Isolation and Partial Characterization of a Cadmium-binding Protein from Pisum sativum" @default.
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