scholarly journals Preparation of Poly(Hydroxamic Acid) for Separation of Zr/Y, Sr System

2011 ◽  
Vol 2011 ◽  
pp. 1-6 ◽  
Author(s):  
Khaled F. Hassan ◽  
Shaban A. Kandil ◽  
Hossam M. Abdel-Aziz ◽  
Tharwat Siyam

Poly(hydroxamic acid) resin (PHA) was prepared by modification of polyacrylamide (PAAm) prepared through -irradiation technique and used for the first time in separation of Zr(IV) from Y(III) and Sr(II) as a simulation mode for the purification of89Zr from its parents (Y or Sr). The adsorption behaviors of zirconium, yttrium, and strontium on the prepared PHA resin in different media, namely, hydrochloric acid, acetate buffer, and citrate buffer were studied as a function of pH. In addition, in cation-exchange column chromatography experiments using PHA, three different eluants, namely,  mol/L HCl, acetate buffer pH 3.5, and 2 mol/L HCl, were employed for elution of Zr(IV), Y(III) and Sr(II), respectively, where Zr(IV), Y(III) and Sr(II) were eluted in amounts of 80%, 99.9%, and 100%, respectively. The purification process of Y(III) from Zr(IV) was carried out using regenerated PHA.

1990 ◽  
Vol 73 (4) ◽  
pp. 627-631
Author(s):  
Edgar C Nicolas ◽  
Kathleen A Pfender ◽  
Michael A Aoun ◽  
Jane E Hemmer

Abstract A fast and simple method for determination of taurine in Infant formulas has been developed. The sample preparation uses disposable ultrafiltration cartridges to remove protein and clarify the sample. Hydrolysis Is avoided, simplifying the procedure and increasing efficiency. One mL sample Is centrlfuged In a cartridge for 45 mln. The filtrate Is diluted with pH 2.2 citrate buffer and Injected into a high performance amino acid analyzer. A cation-exchange column (sodium phase) Is used with a single buffer eluant and an Isocratic chromatographic program. Colorimetrlc detection is performed following post-column nlnhydrln reaction. Chromatographic resolution from other nlnhydrln-posltive compounds is excellent. Average recoveries for 3 levels of spike for various products were 100-102%. Precision Is 1-3% RSD, depending on product. Linearity, specificity, and ruggedness are excellent. The method Is applicable to quality control testing of milk-based, soy-based, and prehydrolyzed proteinbased Infant formulas In the ready-to-use, concentrate, and powder forms. A variety of commercially available Infant formulas from different manufacturers were analyzed and all were found to contain taurine levels comparable to human milk. Some human milk and cow's milk samples were also analyzed and results compare well with literature values


2013 ◽  
Vol 395-396 ◽  
pp. 601-604
Author(s):  
Jian Lan Suo

Objective: Optimizing the extraction of total alkaloids from Caulophyllum robustum. Methods: The taspine which is a type of alkaloids of Caulophyllum robustum is selected as the target index. First, developing the HPLC analysis protocol; second, using orthogonal design method to optimize the hydrochloric acid leaching protocol; third, using cation exchange column to isolate the alkaloids and examining the optimal conditions. Results: the optimal conditions of hydrochloric acid leaching protocol is using 7 column volume of 1% hydrochloric acid for 3 times. The materials are loaded onto the LSD001 cation exchange column with optimal pH 4 and flowrate 2ml/mL, the elution buffer is 10 column volume 5% hydrochloric acid. After desalting, the yield of alkaloids is 1.35% which includes 6.83% of taspine.


1986 ◽  
Vol 51 (4) ◽  
pp. 1032-1036 ◽  
Author(s):  
E. LI-CHAN ◽  
S. NAKAI ◽  
J. SIM ◽  
D.B. BRAGG ◽  
K.V. LO

1989 ◽  
Vol 257 (1) ◽  
pp. 183-186 ◽  
Author(s):  
S Solis-Mendiola ◽  
R Zubillaga-Luna ◽  
A Rojo-Dominguez ◽  
A Hernandez-Arana

Four chymopapain forms were isolated by high-resolution liquid chromatography on a cation-exchange column. The three major forms possess nearly identical secondary and tertiary structures, as judged from their c.d. spectra; these components showed similar proteolytic activity and Mr values close to that of papain. The fourth isolated component seems to be a mixture of modified proteins.


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