Effect of metallic cations on human serum: Study by starch-gel electrophoresis

1967 ◽  
Vol 120 (2) ◽  
pp. 255-267 ◽  
Author(s):  
Koichiro Aoki ◽  
Joji Hori ◽  
Kazuro Kawashima
Keyword(s):  
Human Serum ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Metallic Cations

Ultrasonic Effects on lsoenzymes

1966 ◽  
Vol 12 (4) ◽  
pp. 181-186 ◽  
Author(s):  
Clyde A Dubbs
Keyword(s):  
Human Serum ◽  
Ultrasonic Treatment ◽  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Serum Cholinesterase ◽  
Starch Gel Electrophoresis ◽  
Selective Activation ◽  
Intracellular Enzymes ◽  
Starch Gel

Abstract Several significant effects of ultrasonic treatment on human serum cholinesterase and aminopeptidase isoenzymes and on other serum proteins have been found by starch gel electrophoresis. The selective activation of one cholinesterase isoenzyme is especially striking. These effects must be considered when ultrasonic treatment is used for the extraction of intracellular enzymes. When the effects are appreciated, ultrasonics should provide a valuable tool for isoenzyme research.

Human serum α-1-lipoprotein patterns revealed by starch gel electrophoresis

Lipids ◽  
1968 ◽  
Vol 3 (5) ◽  
pp. 420-424 ◽  
Author(s):  
Louis Cohen ◽  
Juliana Djordjevich
Keyword(s):  
Human Serum ◽  
Gel Electrophoresis ◽  
Starch Gel Electrophoresis ◽  
Starch Gel

scholarly journals HETEROGENEITY OF THE INHERITED GROUP-SPECIFIC COMPONENT OF HUMAN SERUM

1964 ◽  
Vol 120 (1) ◽  
pp. 83-91 ◽  
Author(s):  
Alexander G. Bearn ◽  
F. David Kitchin ◽  
Barbara H. Bowman
Keyword(s):  
Human Serum ◽  
Gel Electrophoresis ◽  
Polypeptide Chain ◽  
Buffer System ◽  
Starch Gel Electrophoresis ◽  
Specific Component ◽  
Agar Gel ◽  
Main Band ◽  
Starch Gel ◽  
Normal Human

Heterogeneity of the group-specific (Gc) components in normal human serum has been demonstrated by the use of a lithium borate buffer system in conventional vertical starch gel electrophoresis and by prolonged immunoelectrophoresis in agar gel. In both Gc 1-1 and Gc 2-2 phenotypes a protein component migrates ahead of the main band. Immunological evidence indicates that the faster migrating band contains Gc specificity. The possibility that the two electrophoretically distinct Gc components share a common polypeptide chain is discussed.

THE ASSOCIATION OF I131-LABELLED THYROXINE AND TRIIODOTHYRONINE WITH SERUM PROTEINS AFTER STARCH GEL ELECTROPHORESIS

1965 ◽  
Vol 43 (9) ◽  
pp. 1477-1487 ◽  
Author(s):  
Amy Britton ◽  
Brian R. Webster ◽  
Calvin Ezrin ◽  
Robert Volpe
Keyword(s):  
Human Serum ◽  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Borate Buffer ◽  
Starch Gel Electrophoresis ◽  
Thyroxine Binding Globulin ◽  
Starch Gel

The binding of I131-labelled triiodothyronine (T3) and 1-thyroxine (T4) with the proteins of human serum has been investigated by means of vertical starch gel electrophoresis in borate buffer at pH 8.6. T3 was found to bind largely to thyroxine-binding globulin (TBG) with very little association with albumin, whereas T4 was associated with TBG, albumin, and thyroxine-binding prealbumin (TBPA). Sera from normal persons were shown to have binding capacities for added thyroxine of 25 μg T4 per 100 ml for TBG, and 40 μg T4 per 100 ml for TBPA.

Fractionation of Plasminogen by Starch Gel Electrophoresis

1964 ◽  
Vol 12 (01) ◽  
pp. 126-136 ◽  
Author(s):  
Karl H. Slotta ◽  
J. D Gonzalez
Keyword(s):  
Gel Electrophoresis ◽  
Room Temperature ◽  
Broad Band ◽  
Caproic Acid ◽  
Starch Gel Electrophoresis ◽  
Full Activity ◽  
Veronal Buffer ◽  
Starch Gel ◽  
Alkaline Range

SummaryWhen urea or ε-amino caproic acid were used as solublizing agents for plasminogen in electrophoretic experiments, only one broad band of the proenzyme was obtained on acetate cellulose, in starch block, and in acrylamide gel. In starch gel electrophoresis, however, both forms of plasminogen – the native or euglobulin and Kline’s or Pseudoglobulin plasminogen – separated into six bands. These migrated toward the cathode at room temperature in borate or veronal buffer in the alkaline range and showed full activity in fibrinagar-streptokinase plates.

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