20152
Chromosorb® W
HP, 60-80 mesh particle size, bottle of 100 g
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化学文摘社编号:
UNSPSC Code:
23151817
PubChem Substance ID:
EC Number:
293-303-4
MDL number:
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Chromosorb is a registered trademark of Imerys Minerals California, Inc.
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Myroslav Sprynskyy et al.
Journal of hazardous materials, 181(1-3), 700-707 (2010-06-15)
In this work the natural and the surfactant modified diatomite has been tested for ability to remove uranium ions from aqueous solutions. Such controlling factors of the adsorption process as initial uranium concentration, pH, contact time and ionic strength have
Guodong Sheng et al.
Environmental science & technology, 45(18), 7718-7726 (2011-08-23)
Sequestration of Ni(II) on diatomite as a function of time, pH, and temperature was investigated by batch, XPS, and EXAFS techniques. The ionic strength-dependent sorption at pH < 7.0 was consistent with outer-sphere surface complexation, while the ionic strength-independent sorption
Myroslav Sprynskyy et al.
Colloids and surfaces. B, Biointerfaces, 94, 7-14 (2012-02-14)
Adsorption kinetics of zearalenone (ZEA) toxin from synthetic gastric fluid (SGF) and synthetic body fluid (SBF) by talc and diatomite was studied in the batch experiments. Chemical composition, morphology and structure of the used adsorbents were examined by scanning electron
Improved performance of diatomite-based dental nanocomposite ceramics using layer-by-layer assembly.
Xiaoli Lu et al.
International journal of nanomedicine, 7, 2153-2164 (2012-05-24)
To fabricate high-strength diatomite-based ceramics for dental applications, the layer-by-layer technique was used to coat diatomite particles with cationic [poly(allylamine hydrochloride)] and anionic [poly(sodium 4-styrenesulfonate)] polymers to improve the dispersion and adsorption of positively charged nano-ZrO(2) (zirconia) as a reinforcing
Junhua Li et al.
Journal of chromatography. B, Analytical technologies in the biomedical and life sciences, 917-918, 30-35 (2013-01-29)
A basic polypeptide L2 (252-273) derived from Escherichia coli ribosomal protein L2 was used as a purification tag. In order to develop faster, less expensive methods for expression and purification of proteins, the L2 (252-273)-small ubiquitin like modifier (SUMO) fusion
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