Growth-inhibitory and metal-binding proteins in Chlorella vulgaris exposed to cadmium or zinc
| Autor: | Gaoling Huang, Bing Shi, Zhiyong Huang, Lianping Li, Xiaoqin Xu, Qingpi Yan |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
chemistry.chemical_classification
Cadmium Chromatography Time Factors Molecular mass Health Toxicology and Mutagenesis Chlorella vulgaris Algal Proteins chemistry.chemical_element Zinc Aquatic Science medicine.disease_cause Mass Spectrometry chemistry Sephadex Zinc toxicity Metalloprotein medicine Metallothionein Water Pollutants Chemical |
| Zdroj: | Aquatic toxicology (Amsterdam, Netherlands). 91(1) |
| ISSN: | 1879-1514 |
| Popis: | Phytochelatins, with the general structure of (gamma-Glu-Cys)n-Gly (n=2-11), are usually recognized as being strongly induced by metals in microalgae and play an important role in the detoxification of heavy metals in environment. However, there have been few studies on metallothionein (MT) synthesis in Chlorella vulgaris (C. vulgaris) exposed to heavy metals. The present study describes the growth inhibition of C. vulgaris exposed to different concentrations of cadmium and zinc, and the induction of metal-binding MT-like proteins in the cells. The amounts of metal-binding proteins, induced in the alga exposed to different concentrations of Cd and Zn, were analyzed with a size-exclusion HPLC coupled to ICP-MS. After being purified with a gel filtration column (Sephadex G-75, 3.5cmx80cm) and a desalting column (G-25, 1.5cmx30cm), the isoforms and sub-isoforms of Zn-binding protein were characterized by a reverse phase-HPLC coupled to electrospray ionization and a triple quadrupole mass spectrometer (HPLC-ESI-MS/MS). In addition, the ultraviolet spectra of purified Zn-binding proteins were analyzed in media with different pH values. The results showed that the significant inhibitory effects (at p |
| Databáze: | OpenAIRE |
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