scholarly journals Supplementary material to "Substantial organic impurities at the surface of synthetic ammonium sulfate particles"

Author(s):  
Junteng Wu ◽  
Nicolas Brun ◽  
Juan Miguel González-Sánchez ◽  
Badr R’Mili ◽  
Brice Temime Roussel ◽  
...  
2021 ◽  
Author(s):  
Junteng Wu ◽  
Nicolas Brun ◽  
Juan Miguel González-Sánchez ◽  
Badr R’Mili ◽  
Brice Temime Roussel ◽  
...  

Abstract. Ammonium sulfate (AS) particles are widely used for studying the physical-chemistry processes of aerosols and for instrument calibrations. Small quantities of organic matter can greatly influence the studied properties, as observed by many laboratory studies. In this work, monodisperse particles (from 200 nm to 500 nm) were generated by nebulizing various AS solutions and organic impurities were quantified relative to sulfate using a High-Resolution Time-of-Flight Aerosol Mass Spectrometer (HR-ToF-AMS). The organic content found in AS solutions was also tentatively identified using a Liquid Chromatography–tandem Mass Spectrometry (LC-MS). The results from both analytical techniques were consistent and demonstrated that the organic impurities contained oxygen, nitrogen and/or sulfur, their molecular masses ranged from m/z 69 to 420, they likely originate from the commercial AS crystals. For AS particle sizes ranging from 200 nm to 500 nm, the total mass fraction of organic (relative to sulfate) ranged from 3.8 % to 1.5 % respectively. An inorganic-organic mixture model suggested that the organic impurities were coated on the AS particle surface with a density of 1.1 × 10−3 g m−2. A series of tests were performed to remove the organic content (using pure N2 in the flow, ultrapure water in the solutions, and very high AS quality), showing that at least 40 % of the organic impurities could be removed. In conclusion, it is recommended to use AS seeds with caution, especially when small particles are used, in terms of AS purity and water purity when aqueous solutions are used for atomization.


1968 ◽  
Vol 20 (03/04) ◽  
pp. 457-464 ◽  
Author(s):  
L Gonyea ◽  
R Herdman ◽  
R. A Bridges

SummaryAn anticoagulant occurring in 4 of 6 patients with SLE has been demonstrated by a sensitive assay utilizing an ammonium sulfate fraction of serum. The anticoagulant functions as an inhibitor of the activation of prothrombin. No species specificity was demonstrable. The inhibitor behaves clinically and chromatographically as an immunoglobulin, although an attempt to demonstrate directly the antibody nature of the inhibitor was not successful.A severe, apparently independent, decrease in the level of prothrombin was observed in the patient with hemorrhagic symptoms. In contrast to the anticoagulant activity, the low prothrombin has persisted during treatment.


2013 ◽  
Vol 10 (2) ◽  
pp. 29
Author(s):  
Normah Ismail ◽  
Nur' Ain Mohamad Kharoe

Unripe and ripe bilimbi (Averrhoa bilimbi L.) were ground and the extracted juices were partially purified by ammonium sulfate precipitation at the concentrations of 40 and 60% (w/v). The collected proteases were analysed for pH, temperature stability, storage stability, molecular weight distribution, protein concentration and protein content. Protein content of bilimbi fruit was 0.89 g. Protease activity of both the unripe and ripe fruit were optimum at pH 4 and 40°C when the juice were purified at 40 and 60% ammonium sulfate precipitation. A decreased in protease activity was observed during the seven days of storage at 4°C. Molecular weight distribution indicated that the proteases protein bands fall between IO to 220 kDa. Protein bands were observed at 25, 50 and 160 kDa in both the unripe and ripe bilimbi proteases purified with 40% ammonium sulfate, however, the bands were more intense in those from unripe bilimbi. No protein bands were seen in proteases purified with 60% ammonium sulfate. Protein concentration was higher for proteases extracted with 40% ammonium sulfate at both ripening stages. Thus, purification using 40% ammonium sulfate precipitation could be a successful method to partially purify proteases from bilimbi especially from the unripe stage. 


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