Formation of Cadmium-Binding Peptide Allomorphs in Fission Yeast
- 1 October 1984
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 96 (5) , 1375-1379
- https://doi.org/10.1093/oxfordjournals.jbchem.a134965
Abstract
It has been reported that two kinds of Cd-binding peptide (Cd-BP1 and Cd-BP2) are induced in fission yeast upon exposure to Cd, and that they consist of the same unit peptide (cadystin), but Cd-BP1 binds 1.5 times more Cd atoms per cadystin than Cd-BP2 (Murasugi, A., Wada, C., & Hayashi, Y. (1981) J. Biochem. 90, 1561–1564). The relative amount of each allomorphic Cd-BP in the cell varied with time after induction and with the concentration of Cd in the induction medium. Further, the production of acid-labile sulfide in the cell increased greatly upon exposure to Cd and varied with time after Cd addition and with Cd concentration in the medium, as in the case of Cd-BP1. Since Cd-BP1 contains labile sulfide, the increase of labile sulfide production together with the increase of cellular Cd concentration may be the driving force to form Cd-BP1, resulting in the increase of the relative amount of Cd-BP1.Keywords
This publication has 5 references indexed in Scilit:
- Purification and unique properties in UV and CD spectra of Cd-binding peptide 1 from SchizosaccharomycespombeBiochemical and Biophysical Research Communications, 1981
- Cadmium-Binding Peptide Induced in Fission Yeast, Schizosaccharomyces pombeThe Journal of Biochemistry, 1981
- Ligand substitution reactions of metallothioneins with EDTA and apo-carbonic anhydrase.Proceedings of the National Academy of Sciences, 1980
- Reactivation in vitro of zinc-requiring apo-enzymes by rat liver zinc-thioneinBiochemical Journal, 1980
- Mouse liver metallothioneins. Purification, molecular weight, amino acid composition, and metal content.Journal of Biological Chemistry, 1978