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Purification and characterization of metallothionein-like cadmium binding protein from Asian periwinkle Littorina brevicula

Title
Purification and characterization of metallothionein-like cadmium binding protein from Asian periwinkle Littorina brevicula
Authors
Park J.-S.Chung S.Park I.-S.Kim Y.Koh C.-H.Lee I.-S.
Ewha Authors
이인숙
SCOPUS Author ID
이인숙scopusscopus
Issue Date
2002
Journal Title
Comparative Biochemistry and Physiology - C Toxicology and Pharmacology
ISSN
1532-0456JCR Link
Citation
vol. 131, no. 4, pp. 425 - 431
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Although mussels and oysters in the ocean are known to act as bioconcentrators for contaminants such as heavy metals, their ability to survive in heavily polluted water is relatively limited. The Asian periwinkle, Littorina brevicula, is one species that can accumulate a variety of environmental heavy metals, and the expression of its metal binding protein (MBP) is induced by cadmium. To better characterize this protein and its detoxification mechanism against cadmium, the present work examined the induction of a cadmium binding protein (Cd-BP) in Littorina brevicula exposed to 400 μg/l CdCl2 for 30 days. The induced Cd-BP was purified by chromatography from the supernatants of homogenized organs (digestive gland, gonad, gill and kidney). This Cd-BP was found to consist of 103 amino acids, was rich in Cys (21 residues), and partial C-terminal sequence obtained by MALDI-TOF MS analysis revealed a Cys-XXX-Cys motif, which resembles a typical feature of mollusc metallothionein (MT). The Cd-BP molecular weight of 9.8 kDa is a little larger than that of other MTs. © 2002 Elsevier Science Inc. All rights reserved.
DOI
10.1016/S1532-0456(02)00029-7
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자연과학대학 > 생명과학전공 > Journal papers
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