A three-factor Doehlert matrix design in optimising the determination of octadecyltrimethylammonium bromide by cation-exchange chromatography with suppressed conductivity detection

2007 ◽  
Vol 597 (1) ◽  
pp. 129-136 ◽  
Author(s):  
Tommaso R.I. Cataldi ◽  
Donatella Orlando ◽  
Donatella Nardiello ◽  
Alessandra Rubino ◽  
Giuliana Bianco ◽  
...  
2020 ◽  
Vol 35 (7) ◽  
pp. 1295-1299
Author(s):  
Lukas Miner ◽  
Diane Beauchemin

Cone corrosion by alkaline solutions with flow injection is prevented using cation-exchange chromatography coupled to inductively coupled plasma mass spectrometry.


1991 ◽  
Vol 58 (3) ◽  
pp. 321-328 ◽  
Author(s):  
Joëlle Léonil ◽  
Daniel Mollé

SummaryCation-exchange chromatography on a Mono S column (Pharmacia) was used to separate macropeptide from whey proteins. Macropeptide was eluted by 0·1 M-NaCl in a 20 mM-KCl–HCl buffer, pH 2. This technique was suitable for quantitative determination of macropeptide in rennet whey and also for following the action of chymosin on κ-casein in skim milk. Precipitation at pH 4·6 was used to remove residual caseins and to keep macropeptide in solution. In comparison with other methods for determining macropeptide, the present one eliminates the need for pretreatment of samples with trichloroacetic acid (TCA) and allows the recovery of all the macropeptide. Quantitative determination of macropeptide in the 8% TCA-soluble fraction by cation-exchange chromatography showed that only 50–75% of the macropeptide was recovered. This chromatographic technique could also be applied for isolating and producing whole macropeptide on a preparative scale.


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