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等級
for fluorescence
化驗
≥98.5% (TLC)
形狀
solid
mp
218-221 °C (lit.)
SMILES 字串
CN(C)c1cccc2c(cccc12)S(N)(=O)=O
InChI
1S/C12H14N2O2S/c1-14(2)11-7-3-6-10-9(11)5-4-8-12(10)17(13,15)16/h3-8H,1-2H3,(H2,13,15,16)
InChI 密鑰
TYNBFJJKZPTRKS-UHFFFAOYSA-N
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其他說明
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产品编号
说明
价格
儲存類別代碼
13 - Non Combustible Solids
水污染物質分類（WGK）
WGK 3
閃點（°F）
Not applicable
閃點（°C）
Not applicable
個人防護裝備
Eyeshields, Gloves, type N95 (US)
K Yamasaki et al.
Biochimica et biophysica acta, 1432(2), 313-323 (1999-07-17)
The relationship between the two principal ligand binding sites, sites I and II, on human serum albumin (HSA) was quantitatively and qualitatively examined by equilibrium dialysis and fluorescence spectroscopy. Among the three subsite markers to site I, only the binding
Yasmina S N Day et al.
Protein science : a publication of the Protein Society, 11(5), 1017-1025 (2002-04-23)
The binding interactions of small molecules with carbonic anhydrase II were used as model systems to compare the reaction constants determined from surface- and solution-based biophysical methods. Interaction data were collected for two arylsulfonamide compounds, 4-carboxybenzenesulfonamide (CBS) and 5-dimethyl-amino-1-naphthalene-sulfonamide (DNSA)
Konstantinos Kavallieratos et al.
Journal of the American Chemical Society, 127(18), 6514-6515 (2005-05-05)
The (bis)dansylated sulfonamide 1,2-C6H4(NHSO2C10H6-5-N(CH3)2)2 (1) extracted Pb(II) selectively from water into 1,2-dichloroethane via an ion-exchange mechanism and showed fluorescence quenching upon Pb(II) extraction. The distribution ratios for metal extraction (determined by ICP-MS) for Pb(II) were 133-1410 times higher than those
N Tanaka et al.
Biochimica et biophysica acta, 1338(1), 13-20 (1997-03-07)
The structure of human serum albumin (HSA) in the pressure-induced denatured state was investigated by fluorescence spectroscopy. HSA undergoes a conformational change in the pressure range from 0.1 MPa to 400 MPa, at 25 degrees C. Several ligands bind to
R W Henkens et al.
Biochemistry, 21(23), 5918-5923 (1982-11-09)
Particularly stable elements of noncovalent structure in bovine carbonic anhydrase have been detected and studied. These are present in a highly populated intermediate state formed during denaturation of the enzyme with guanidinium chloride. The intermediate has been detected by analysis
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