64430
DL-Methionine sulfoxide
≥98.5% (NT)
Sinónimos:
dl-Methionine sulfoxide
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About This Item
Productos recomendados
Quality Level
assay
≥98.5% (NT)
reaction suitability
reaction type: solution phase peptide synthesis
mp
~240 °C (dec.)
application(s)
peptide synthesis
SMILES string
CS(=O)CCC(N)C(O)=O
InChI
1S/C5H11NO3S/c1-10(9)3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)
InChI key
QEFRNWWLZKMPFJ-UHFFFAOYSA-N
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Categorías relacionadas
General description
DL-Methionine sulfoxide is an oxidation product of DL-methionine.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Analytical biochemistry, 421(2), 767-769 (2012-01-11)
Study of the posttranslational modification of methionine to its sulfoxide has been receiving increasing attention because of its implication in regulation of protein activity, but techniques for the detection of this modification remain limited. In particular, there has been no
Journal of neuroscience research, 91(5), 706-716 (2013-02-14)
Alzheimer disease (AD) affects mainly people over the age of 65 years, suffering from different clinical symptoms such as progressive decline in memory, thinking, language, and learning capacity. The toxic role of β-amyloid peptide (Aβ) has now shifted from insoluble
PloS one, 8(2), e56064-e56064 (2013-02-26)
Leishmania are protozoan parasites that proliferate within the phagolysome of mammalian macrophages. While a number of anti-oxidant systems in these parasites have been shown to protect against endogenous as well as host-generated reactive oxygen species, the potential role of enzymes
Journal of cosmetic science, 63(6), 359-364 (2013-01-05)
Environmental trauma to human skin can lead to oxidative damage of proteins and affect their activity and structure. When methionine becomes oxidized to its sulfoxide form, methionine sulfoxide reductase A (MSRA) reduces it back to methionine. We report here the
The journal of physical chemistry. B, 115(29), 9202-9212 (2011-07-05)
The hybrid density functional theory method B3LYP in combination with three systematically larger active site models has been used to investigate the substrate binding and catalytic mechanism by which Neisseria gonorrhoeae methionine sulfoxide reductase B (MsrB) reduces methionine-R-sulfoxide (Met-R-SO) to
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