Identification of human serum proteins binding iron, copper, and thyroid hormones by starch gel electrophoresis

1959 ◽  
Vol 15 (7) ◽  
pp. 281-284 ◽  
Author(s):  
A. C. Allison
1966 ◽  
Vol 12 (4) ◽  
pp. 181-186 ◽  
Author(s):  
Clyde A Dubbs

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.


1965 ◽  
Vol 43 (9) ◽  
pp. 1477-1487 ◽  
Author(s):  
Amy Britton ◽  
Brian R. Webster ◽  
Calvin Ezrin ◽  
Robert Volpe

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.


Nature ◽  
1963 ◽  
Vol 197 (4873) ◽  
pp. 1201-1201 ◽  
Author(s):  
R. K. SCOPES

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