Disc Electrophoresis of Proteins from Juvenile and Adult Specimens of Ivy

Nature ◽  
1966 ◽  
Vol 212 (5061) ◽  
pp. 516-517 ◽  
Author(s):  
H. FUKASAWA
Keyword(s):  
Disc Electrophoresis ◽  
Electrophoresis Of Proteins

scholarly journals Double-disc Electrophoresis of Proteins

Nature ◽  
1967 ◽  
Vol 213 (5079) ◽  
pp. 922-922 ◽  
Author(s):  
DAVID RACUSEN
Keyword(s):  
Disc Electrophoresis ◽  
Electrophoresis Of Proteins

scholarly journals Acrylamide gel electrophoresis of proteins, acid phosphatases and RN-ases from three potato varieties

2015 ◽  
Vol 41 (1) ◽  
pp. 107-112 ◽  
Author(s):  
A. Kubicz ◽  
E. Wieczorek ◽  
B. Morawiecka
Keyword(s):  
Solanum Tuberosum ◽  
Acid Phosphatase ◽  
Relative Abundance ◽  
Gel Electrophoresis ◽  
Acid Phosphatase Activity ◽  
Disc Electrophoresis ◽  
Acid Phosphatases ◽  
Main Zone ◽  
Activity Distribution ◽  
Electrophoresis Of Proteins

Studies on variety differences in the protein and acid phosphatase patterns as well as ribunuclease activity distribution were carried out by disc electrophoresis on saline extracts of three varieties of the potato <i>Solanum tuberosum</i> (L.). The protein bands varied in number, position and relative abundance. One main zone of the acid phosphatase activity was detected consisting of 2-3 electrophoretically different bands. Variety differences were concerned with the number and relative abundance of these bands. RNase activity was detected in 4 main zones, in some of them additional subbands were visible. Differences between the three examined varieties were reflected in the occurence of the particular activity zones or their subbands.

The Effect of Antithrombin III on the Activity of the Coagulation Factors VII, IX and X

1976 ◽  
Vol 35 (02) ◽  
pp. 295-304 ◽  
Author(s):  
B Østerud ◽  
M Miller-Andersson ◽  
U Abildgaard ◽  
H Prydz
Keyword(s):  
Antithrombin Iii ◽  
Factor Xa ◽  
Coagulation Factors ◽  
Disc Electrophoresis ◽  
Polyacrylamide Gel ◽  
Factor Vii ◽  
Native Form ◽  
Factor Ixa ◽  
Plasma Factor

SummaryAntithrombin III, purified to homogeneity according to Polyacrylamide gel disc electrophoresis and immunoelectrophoresis, inhibited the activity of purified factor IXa and Xa, whereas factor VII was not inhibited either in the active or in the native form.Antithrombin III is the single most important inhibitor of factor Xa in plasma. Factor Xa does not, however, reduce the activity of antithrombin III against thrombin.

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