Isolation and spectral characterization of cadmium binding metallothionein

Abstract A cadmium (Cd)-binding protein was isolated and characterized from the Antarctic clam Laternula elliptica after experimental exposure to a high concentration of Cd. Cd-binding metallothioneins (MTs) in the cytosol were purified using a procedure based on gel permeation and ion-exchange chro...

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Bibliographic Details
Published in:Antarctic Science
Main Authors: Park, Hyun, Ahn, In-Young, Choi, Heeseon J., Ji, Jung Youn
Format: Article in Journal/Newspaper
Language:English
Published: Cambridge University Press (CUP) 2007
Subjects:
Geology
Ecology, Evolution, Behavior and Systematics
Oceanography
Antarctic
The Antarctic
Antarc*
Antarctic Science
Online Access:http://dx.doi.org/10.1017/s0954102007000806
https://www.cambridge.org/core/services/aop-cambridge-core/content/view/S0954102007000806
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Summary:Abstract A cadmium (Cd)-binding protein was isolated and characterized from the Antarctic clam Laternula elliptica after experimental exposure to a high concentration of Cd. Cd-binding metallothioneins (MTs) in the cytosol were purified using a procedure based on gel permeation and ion-exchange chromatography. The purified MTs were recognized by MT antibodies in a Western blotting assay. MALDI-TOF MS analyses showed that the molecular mass of the purified MTs was 7.27 kDa, which is typical of MTs found in marine invertebrates. The Cd binding to MT, reflected by the redistribution of Cd ions, was monitored by spectrophotometry. The absorption spectra profiles indicated the presence of Cd-MT complexes, and a 4 nm red shift of the unresolved lowest energy-absorption band occurred when five equivalents of Cd (II) were incorporated.

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