High-resolution capillary electrophoretic analysis of DNA in free solution

1992 ◽  
Vol 13 (1) ◽  
pp. 18-31 ◽  
Author(s):  
Suraphol Nathakarnkitkool ◽  
Peter J. Oefner ◽  
Georg Bartsch ◽  
Mihael A. Chin ◽  
Günther K. Bonn
1999 ◽  
Vol 20 (7) ◽  
pp. 1373-1381 ◽  
Author(s):  
Katherine M. Williams ◽  
Jörgen Ekström ◽  
Thomas Marshall

2010 ◽  
Vol 6 (2) ◽  
pp. 181-185 ◽  
Author(s):  
Noor Fitri ◽  
Björn Thiele ◽  
Klaus Günther ◽  
Buchari Buchari

A capillary electrophoretic (CE) analysis with ultra-violet (UV) detection was performed for further separation of low-molecular-mass (LMM) calcium species in phloem sap of Ricinus communis L. Two different background electrolytes (BGE) were used for the separation; these are (1) hydrogen phosphate/dihydrogen phosphate buffer containing cetyltrimethylammonium bromide (CTAB) as an electro-osmotic flow (EOF) modifier, and (2) boric acid buffer containing CTAB. Various parameters affecting the analysis, including the composition and pH of the BGE were systematically studied. The sensitivity, resolution, baseline noise, migration time of the species peaks, and reproducibility of the method were evaluated under optimised condition. At least 13 UV-active species were optimally separated within about ten minutes. The optimised measurement condition was also achieved using 10 mM hydrogen phosphate/10 mM dihydrogen phosphate containing 0.5 mM CTAB at pH 8.0 as BGE, and by applying voltage of ‑20 kV and temperature of 14°C. Evidently, the analytical method was successfully used for the separation of LMM calcium species in phloem sap of R. communis L.   Keywords: capillary electrophoresis, calcium species, phloem sap, Ricinus communis


1998 ◽  
Vol 19 (8-9) ◽  
pp. 1270-1274 ◽  
Author(s):  
Hideyuki Kajiwara ◽  
Andrew M. Hemmings

1974 ◽  
Vol 187 (1088) ◽  
pp. 353-361 ◽  

The intact chromaffin granule has been studied by high resolution proton and phosphorus magnetic resonance spectroscopy. In the granule the proton peaks of adrenaline and ATP are shifted upfield differentially with respect to their positions in free solution. All lines in both proton and phosphorus magnetic resonance spectra were considerably broadened. The n.m.r. spectrum of the chromogranin protein in the vesicles was also well resolved. A structure of the vesicle is proposed.


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