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等级
ACS reagent
puriss. p.a.
检测方案
≥99.0% (NT)
形式
solid
自燃温度
1112 °F
缺失
≤1% loss on drying, 130 °C
pH值(酸碱度)
7.0-9.2 (25 °C, 50 mg/mL in H2O)
pKa
4.76 (acetic acid)
mp
>300 °C (dec.) (lit.)
溶解性
ethanol: soluble(lit.)
water: soluble(lit.)
痕量阴离子
chloride (Cl-): ≤20 mg/kg
phosphate (PO43-): ≤5 mg/kg
sulfate (SO42-): ≤20 mg/kg
痕量阳离子
Al: ≤5 mg/kg
Ca: ≤10 mg/kg
Cd: ≤5 mg/kg
Co: ≤5 mg/kg
Cr: ≤5 mg/kg
Cu: ≤5 mg/kg
Fe: ≤5 mg/kg
K: ≤200 mg/kg
Mg: ≤5 mg/kg
Mn: ≤5 mg/kg
Ni: ≤5 mg/kg
Pb: ≤5 mg/kg
Zn: ≤5 mg/kg
SMILES字符串
[Na+].CC([O-])=O
InChI
1S/C2H4O2.Na/c1-2(3)4;/h1H3,(H,3,4);/q;+1/p-1
InChI key
VMHLLURERBWHNL-UHFFFAOYSA-M
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一般描述
Sodium acetate is a colorless compound and its crystals belong to the monoclinic crystal system. Sodium acetate trihydrate can be obtained from the crystallization of sodium acetate in water. Its trihydrate loses water of crystallization on heating at 75°C, while on heating above 120°C, anhydrous sodium acetate is obtained. It can be synthesized by reacting sodium carbonate or sodium hydroxide with acetic acid. It is widely employed in the organic laboratory for the preparation of buffer solutions. It has been reported to inhibit the growth of Listeria monocytogenes.
应用
Sodium acetate may be used in the following studies:
- Separation and quantification of tartrazine (E 102), amaranth (E 123), erythrosine (E 127) and indigotine (E 132) in soft drinks by reverse phase HPLC method.
- Preparation of guanidine solution required for the total RNA preparation.
- Enantiomeric enrichment of (2S)-2-methyl-2-(2-propen-1-yl)-cyclohexanone.
其他说明
This product has been replaced by 32319-Sigma-Aldrich | Sodium acetate, puriss. p.a., ACS reagent, reag. Ph. Eur., anhydrous | CH3COONa
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
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The liquid-chromatographic quantification of some synthetic colorants in soft drinks.
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Listeria monocytogenes inhibition in refrigerated vacuum packaged turkey bologna by chemical additives.
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The formation of β-sheet rich prion oligomers and fibrils from native prion protein (PrP) is thought to be a key step in the development of prion diseases. Many methods are available to convert recombinant prion protein into β-sheet rich fibrils
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