Microchip analysis of lithium in blood using moving boundary electrophoresis and zone electrophoresis

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

Sex and sex-cycle differences in rat serum protein concentrations

1959 ◽  
Vol 197 (1) ◽  
pp. 135-137 ◽  
Author(s):  
Werner G. Heim
Keyword(s):  
Moving Boundary ◽  
Serum Proteins ◽  
Female Rats ◽  
Estrus Cycle ◽  
Rat Serum ◽  
Male And Female ◽  
Male And Female Rats ◽  
Blood Serum Proteins ◽  
Zone Electrophoresis ◽  
Sex Cycle

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.

2D separations on a 1D chip: gradient elution moving boundary electrophoresis—chiral capillary zone electrophoresis

Lab on a Chip ◽  
2010 ◽  
Vol 10 (22) ◽  
pp. 3139 ◽  
Author(s):  
David Ross ◽  
Jonathan G. Shackman ◽  
Jason G. Kralj ◽  
Javier Atencia
Keyword(s):  
Capillary Zone Electrophoresis ◽  
Moving Boundary ◽  
Gradient Elution ◽  
Zone Electrophoresis ◽  
Capillary Zone

THE PROTEOLYTIC ENZYMES OF MICROORGANISMS: VI. THE SEPARATION OF PROTEASES FROM MORTIERELLA RENISPORA DIXON-STEWART BY ZONE ELECTROPHORESIS

1954 ◽  
Vol 32 (1) ◽  
pp. 20-26 ◽  
Author(s):  
L. R. Wetter
Keyword(s):  
Filter Paper ◽  
Active Component ◽  
Culture Medium ◽  
Moving Boundary ◽  
Proteolytic Enzymes ◽  
Potato Starch ◽  
Paper Electrophoresis ◽  
Active Components ◽  
Zone Electrophoresis ◽  
The Difference

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.

THE PROTEOLYTIC ENZYMES OF MICROORGANISMS: VI. THE SEPARATION OF PROTEASES FROM MORTIERELLA RENISPORA DIXON-STEWART BY ZONE ELECTROPHORESIS

1954 ◽  
Vol 32 (1) ◽  
pp. 20-26 ◽  
Author(s):  
L. R. Wetter
Keyword(s):  
Filter Paper ◽  
Active Component ◽  
Culture Medium ◽  
Moving Boundary ◽  
Proteolytic Enzymes ◽  
Potato Starch ◽  
Paper Electrophoresis ◽  
Active Components ◽  
Zone Electrophoresis ◽  
The Difference

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.

An Automated Valve for Dispersion Control in On-Chip Electrophoresis

2007 ◽  
Author(s):  
Huanchun Cui ◽  
Prashanta Dutta ◽  
Cornelius F. Ivory
Keyword(s):  
Control System ◽  
Moving Boundary ◽  
Mechanical Valve ◽  
Side Channel ◽  
Automated Control ◽  
Automated Control System ◽  
Band Dispersion ◽  
Zone Electrophoresis ◽  
Electrokinetic Separations ◽  
On Chip

Band dispersion and sample loss into a side channel is a major problem when an electrokinetically-mobilized concentration zone passes a T-junction in a networked microfluidic chip. The band dispersion can be minimized in linear electrophoretic systems such as zone electrophoresis and moving boundary electrophoresis by applying a constant additional electric field in the side channel. However, constant valve voltages have shown to provide unsatisfactory valve performance during nonlinear electrophoresis (isotachophoresis). In this study, an automated valve system was developed to reduce the band dispersion at the intersection during non-linear electrophoresis. The automated valve consists of two integrated microelectrodes and a control system. With the automated control system, two integrated microelectrodes provide an effective way to manipulate current streamlines, thus acting as a non-mechanical valve for charged species in electrokinetic separations. Experimental results with this non-mechanical valve show decreased dispersion and increased reproducibility as protein zones isotachophoretically passed the T-junction.

ISOLEMENT ET QUELQUES CARACTERISTIQUES D'UNE GONADOTROPHINE URINAIRE DE MÉNOPAUSE HOMOGÈNE A L'ELECTROPHORÈSE

1960 ◽  
Vol XXXV (II) ◽  
pp. 225-234 ◽  
Author(s):  
R. Bourrillon ◽  
R. Got ◽  
R. Marcy
Keyword(s):  
Sialic Acid ◽  
Histological Study ◽  
Active Material ◽  
Biologically Active ◽  
New Method ◽  
Female Rats ◽  
Mouse Uterus ◽  
Highly Active ◽  
Zone Electrophoresis ◽  
Human Menopausal Gonadotrophin

ABSTRACT A new method for preparation of Human Menopausal Gonadotrophin involves successively alcoholic precipitation, kaolin adsorption and chromatography on ion exchangers. A highly active material is obtained which corresponds to 1 mg per litre of urine and has an activity of 1 mouse uterus unit at a dose of 0.003 mg. This gonadotrophin possesses both follicle stimulating and luteinizing activities in hypophysectomized female rats, by histological study. It contains 13 % hexose, 10% hexosamine and 8.5 % sialic acid. A further purification, by zone electrophoresis on starch, gives a final product, biologically active at 0.001 mg, which behaves as an homogenous substance in free electrophoresis with mobility −4.76 × 10−5 at pH 8.6.

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