Two proteins of low molecular weight, which bind cadmium and are rich in cysteine were isolated from kidneys of the striped dolphin, Stenella coeruleoalba, and identified as metallothioneins I and II. The two isoforms closely resembled horse renal isometallothioneins both in chromatographic behaviors and chemical compositions. The molecular weights of performic acidoxidized proteins were estimated to be 6,800. Twenty to 21 cysteine residues and about 6 g-atoms of heavy metals (Zn, Cd, Cu, and Hg) were present per mole of each isomer. © 1986, Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.
CITATION STYLE
Kwohn, Y. T., Yamazaki, S., Okubo, A., Yoshimura, E., Tatsukawa, R., & Toda, S. (1986). Isolation and Characterization of Metallothionein from Kidney of Striped Dolphin, Stenella coeruleoalba. Agricultural and Biological Chemistry, 50(11), 2881–2885. https://doi.org/10.1271/bbb1961.50.2881
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