Step width, spacing, and resolution in gradient elution moving boundary electrophoresis. Part 1. Theory and comparison with zone electrophoresis

2010 ◽  
Vol 31 (22) ◽  
pp. 3650-3657 ◽  
Author(s):  
David Ross
Lab on a Chip ◽  
2010 ◽  
Vol 10 (22) ◽  
pp. 3139 ◽  
Author(s):  
David Ross ◽  
Jonathan G. Shackman ◽  
Jason G. Kralj ◽  
Javier Atencia

2005 ◽  
Vol 26 (15) ◽  
pp. 3032-3042 ◽  
Author(s):  
Elwin X. Vrouwe ◽  
Regina Luttge ◽  
Wouter Olthuis ◽  
Albert van den Berg

2011 ◽  
Vol 83 (16) ◽  
pp. 6316-6322 ◽  
Author(s):  
Elizabeth A. Strychalski ◽  
Alyssa C. Henry ◽  
David Ross

1959 ◽  
Vol 197 (1) ◽  
pp. 135-137 ◽  
Author(s):  
Werner G. Heim

The relative concentrations of the various blood serum proteins, and especially of albumin, were found to be significantly different in male and female rats when examined by moving boundary or zone electrophoresis. However, no significant differences were noted in the sera obtained from rats at different points in the estrus cycle.


1954 ◽  
Vol 32 (1) ◽  
pp. 20-26 ◽  
Author(s):  
L. R. Wetter

Moving-boundary electrophoresis indicated that a protease concentrate obtained from the culture medium of Mortierella renispora Dixon-Stewart (PRL 26) was made up of a number of proteins. Filter-paper electrophoresis demonstrated that two of the proteins were capable of hydrolyzing denatured hemoglobin. One active component had a negative mobility, the other a positive mobility in phosphate buffer pH 6.8, ionic strength 0.1. Because of the difference in electrical properties it was possible to separate the two active components by zone electrophoresis. Though yields were low when filter paper was employed, the use of potato starch as the supporting medium resulted in excellent recoveries.


1954 ◽  
Vol 32 (1) ◽  
pp. 20-26 ◽  
Author(s):  
L. R. Wetter

Moving-boundary electrophoresis indicated that a protease concentrate obtained from the culture medium of Mortierella renispora Dixon-Stewart (PRL 26) was made up of a number of proteins. Filter-paper electrophoresis demonstrated that two of the proteins were capable of hydrolyzing denatured hemoglobin. One active component had a negative mobility, the other a positive mobility in phosphate buffer pH 6.8, ionic strength 0.1. Because of the difference in electrical properties it was possible to separate the two active components by zone electrophoresis. Though yields were low when filter paper was employed, the use of potato starch as the supporting medium resulted in excellent recoveries.


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