Cloning, characterization, and expression of cadmium-induced metallothionein-2 gene from earthworm Pheretima aspergillum (E. Perrier)
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چکیده
منابع مشابه
Earthworm (Pheretima aspergillum) extract stimulates osteoblast activity and inhibits osteoclast differentiation
BACKGROUND The potential benefits of earthworm (Pheretima aspergillum) for healing have received considerable attention recently. Osteoblast and osteoclast activities are very important in bone remodeling, which is crucial to repair bone injuries. This study investigated the effects of earthworm extract on bone cell activities. METHODS Osteoblast-like MG-63 cells and RAW 264.7 macrophage cell...
متن کاملEffect of oral administration of Pheretima aspergillum (earthworm) in rats with cerebral infarction induced by middle-cerebral artery occlusion.
We investigated the curative effect of Pheretima aspergillum (earthworm, PA) on rats with middle cerebral artery occlusion (MCAo). The MCAo-induced cerebral infarction was established and its underlying mechanisms by counting the infarction areas and evaluating the rats' neurological status. Immunostaining was used to test the expression of NeuN, and glial fibrillary acidic (GFAP), S100B, and b...
متن کاملCloning and Expression Analysis of ZmERD3 Gene From Zea mays
Background: Stresses (such as drought, salt, viruses, and others) seriously affect plant productivity. To cope with these threats, plants express a large number of genes, including several members of ERD (early responsive to dehydration) genes to synthesize and assemble adaptive molecules. But, the function of ERD3 gene hasn’t been known so far.Objectives:</strong...
متن کاملPurification, Characterization, and cDNA Cloning of a Novel Metallothionein-like, Cadmium-binding Protein from
Caenorhabditis elegans adapted for survival in high concentrations of Cd(I1) express a heavy metal binding protein designated C. elegans metallothionein-like protein or MT-Ce. This protein was purified to homogeneity and characterized. MT-Ce binds 6 mol of Cd(II)/ mol protein. The sequence of 39 amino-terminal residues in MT-Ce was determined. A radiolabeled 41-mer oligonucleotide, designed fro...
متن کاملPurification, characterization, and cDNA cloning of a novel metallothionein-like, cadmium-binding protein from Caenorhabditis elegans.
Caenorhabditis elegans adapted for survival in high concentrations of Cd(II) express a heavy metal binding protein designated C. elegans metallothionein-like protein or MT-Ce. This protein was purified to homogeneity and characterized. MT-Ce binds 6 mol of Cd(II)/mol protein. The sequence of 39 amino-terminal residues in MT-Ce was determined. A radiolabeled 41-mer oligonucleotide, designed from...
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ژورنال
عنوان ژورنال: Genetics and Molecular Research
سال: 2015
ISSN: 1676-5680
DOI: 10.4238/2015.december.14.5