Results 21 to 30 of about 11,558 (176)

Density and intensity of metallothionein of Crassostrea sp. as biomarkers of heavy metal contamination in the Northern coast of East Java, Indonesia

open access: yesEgyptian Journal of Aquatic Research, 2021
The present study aimed to observe the expression level of metallothionein by analyzing its density and intensity in the gill and stomach of Crassostrea glomerata and Crassostrea iredalei.
Asus Maizar Suryanto Hertika   +3 more
doaj   +1 more source

Copper metallothioneins [PDF]

open access: yesIUBMB Life, 2017
Abstract Metallothioneins (MTs) are a class of low molecular weight and cysteine‐rich metal binding proteins present in all the branches of the tree of life. MTs efficiently bind with high affinity several essential and toxic divalent and monovalent transition metals by forming characteristic polynuclear metal‐thiolate clusters within
Jenifer, Calvo   +2 more
openaire   +2 more sources

Anti-metallothionein IgG and levels of metallothionein in autistic children with GI disease [PDF]

open access: yes, 2009
A J RussoMount Saint Mary’s University, Emmitsburg, MD, USAAim: To assess both serum concentration of metallotionein (MT) and anti-metallothionein (anti-MT) immunoglobulin G (IgG) in autistic children with gastrointestinal (GI) symptoms and ...
Anthony Russo, A J Russo
core   +1 more source

Metallothionein

open access: yesExperimental Biology and Medicine, 1987
Early research on metallothionein centered on aspects related to a detoxification role. As our understanding of the complex endocrine control that regulates metallothionein gene expression increases, a wider appreciation of a functional role(s) is emerging.
M A, Dunn, T L, Blalock, R J, Cousins
openaire   +2 more sources

Metallothionein: An overview [PDF]

open access: yesWorld Journal of Gastroenterology, 2007
Metallothioneins (MTs) were discovered in 1957 by Margoshes and Vallee and identified as low-molecular weight and sulphydryl rich proteins. It is not surprising that most mammalian tissues contain age related basal levels of MTs since they are involved in metalloregulatory processes that include cell growth and multiplication.
N, Thirumoorthy   +4 more
openaire   +2 more sources

Metallothionein expression in feline injection site fibrosarcomas

open access: yesBMC Veterinary Research, 2023
Background Feline injection site fibrosarcoma is an aggressive and infiltrative tumour arising in the background of chronic inflammation. The aim of this study was to evaluate the expression of metallothionein (I-II) in feline injection site ...
Mateusz Mikiewicz   +4 more
doaj   +1 more source

The Evolution of Insect Metallothioneins [PDF]

open access: yesProceedings of the Royal Society B: Biological Sciences, 2020
ABSTRACT Metallothioneins (MTs) are a family of cysteine-rich metal-binding proteins that are important in the chelating and detoxification of toxic heavy metals. Until now, the short length and the low sequence complexity of MTs has hindered the possibility of any phylogenetic reconstruction, hampering the study of ...
Mei Luo   +4 more
openaire   +2 more sources

Evaluation of metallothionein response in Lymnaea stagnalis pond snail to exposured to trace metals and thiocarbamate fungicide

open access: yesБіологічні студії, 2019
Pulmonate mollusks posses high uptake rates of dissolved metals and their bonding, mainly Cd, Zn and Cu by the metal-buffering protein, metallothionein (MT).
L. L. Gnatyshyna
doaj   +1 more source

Experimental study of metallothionein synthesis in modeling hyperthermic intraoperative intraperitoneal chemoperfusion with cysplatinum

open access: yesJournal of Education, Health and Sport, 2018
In an experiment on white wild-type laboratory rats, it was shown that 90 minutes after intraperitoneal administration of cisplatin at a dose of 4 mg / kg as a solution heated to 43 °C, the integral level of metallothionein significantly increased in the
E. D. Pykhtieieva   +2 more
doaj   +3 more sources

Bacterium-Based Heavy Metal Biosorbents: Enhanced Uptake of Cadmium by E. coli Expressing a Metallothionein Fused to β-Galactosidase

open access: yesBioTechniques, 2002
We investigated the potential utility of a recombinant E. coli that expresses the human metallothionein II gene as a fusion protein with β-galactosidase as a heavy metal biosorbent. E.
N. Yoshida   +5 more
doaj   +1 more source

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