About This Item
Fórmula linear:
C3H6NO6SK
Número CAS:
Peso molecular:
223.25
Número MDL:
Código UNSPSC:
12352300
ID de substância PubChem:
NACRES:
NA.23
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temperatura de armazenamento
2-8°C
cadeia de caracteres SMILES
[K+].N[C@@H](COS([O-])(=O)=O)C(O)=O
InChI
1S/C3H7NO6S.K/c4-2(3(5)6)1-10-11(7,8)9;/h2H,1,4H2,(H,5,6)(H,7,8,9);/q;+1/p-1/t2-;/m0./s1
chave InChI
LXIPCUMLLKNUSU-DKWTVANSSA-M
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
Certificados de análise (COA)
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J Kunert
Journal of basic microbiology, 25(2), 111-118 (1985-01-01)
The dermatophyte Microsporum gypseum was cultivated on a glucose-arginine medium supplemented with five strongly acidic derivatives of cysteine (L-cysteine sulfinic acid, L-cysteic acid, L-serine-O-sulfate and taurine at a concentration of 5 mmol/l, and L-S-sulfocysteine at a concentration of 2.5 mmol/l).
K J Koller et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 5(11), 2882-2888 (1985-11-01)
[3H]-N-Acetylaspartylglutamate (NAAG) bound saturably and reversibly to crude synaptosomal rat brain membranes. Optimal binding occurred in Tris-HCl buffer, pH 7.2, at 37 degrees C using previously frozen, preincubated membranes. Saturation experiments revealed an apparent KD of 383 +/- 33 nM
H Ueno et al.
Biochemistry, 21(18), 4387-4393 (1982-08-31)
The reaction of serine O-sulfate with cytosolic aspartate aminotransferase [John, R.A., & Fasella, P. (1969) Biochemistry 8, 4477] has been reinvestigated. As in the corresponding reaction with beta-chloroalanine [Morino, Y., Osman, A.M., & Okamoto, M. (1974) J. Biol. Chem. 249
Chizuru Nagayoshi et al.
Protein and peptide letters, 16(2), 201-206 (2009-02-10)
We have successfully expressed an active human brain serine racemase (hSR) with His-tag using moderate halophile. The purified His-hSR showed high elimination and racemization activities on L-serine: the elimination activity was 2.6-fold higher than racemization activity. Both enzyme activities showed
R Contestabile et al.
European journal of biochemistry, 240(1), 150-155 (1996-08-15)
The ability of aspartate aminotransferase to catalyse beta-elimination of alpha-amino acids that have a good leaving group at C beta has been exploited in the synthesis of novel amino acids by the inclusion of appropriate nucleophiles as co-substrates. Two compounds
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