Analysis of fish and squid myofibrillar proteins by capillary sodium dodecyl sulfate gel electrophoresis: actin and myosin quantification

2000 ◽  
Vol 211 (6) ◽  
pp. 443-448 ◽  
Author(s):  
C. G. Sotelo ◽  
Carmen Piñeiro ◽  
Ricardo I. Pérez-Martín ◽  
Jose Manuel Gallardo
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Myofibrillar Proteins ◽  
Dodecyl Sulfate

Electrophoresis of Fish Myofibrillar Proteins With Sodium-Dodecyl Sulfate-Polyacrylamide Gel

1973 ◽  
Vol 30 (5) ◽  
pp. 706-707 ◽  
Author(s):  
E. A. Childs
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Phosphate Buffer ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Myofibrillar Proteins ◽  
Electrophoretic Separation ◽  
Dodecyl Sulfate

A method for electrophoretic separation of fish myofibrillar proteins is described. After incubation in phosphate buffer containing β-mercaptoethanol, sodium-dodecyl sulfate (SDS), and urea, the proteins are separated by SDS-acrylamide gel electrophoresis.

Effect of thyroid hormone on carbohydrate content of Na+-K+-adenosine triphosphatase

1984 ◽  
Vol 247 (3) ◽  
pp. C282-C287 ◽  
Author(s):  
C. S. Lo ◽  
L. E. Klein ◽  
T. N. Lo
Keyword(s):  
Thyroid Hormone ◽  
Sodium Dodecyl Sulfate ◽  
Rate Constant ◽  
Gel Electrophoresis ◽  
Adenosine Triphosphatase ◽  
Sodium Dodecyl ◽  
Carbohydrate Content ◽  
Beta Subunits ◽  
Reverse T3 ◽  
Dodecyl Sulfate

The effect of L-3,5,3'-triiodothyronine (T3) (50 micrograms/100 body wt) on the incorporation of labeled glucosamine and fucose into the subunits of Na+-K+-ATPase was examined by gel electrophoresis in sodium dodecyl sulfate. T3 augmented the incorporation of glucosamine into the alpha- and beta-subunits by 51 and 58%, respectively, in the 22-h chase experiments. Similarly T3 augmented the incorporation of fucose into the alpha- and beta-subunits by 58 and 43%, respectively. Reverse T3 did not alter the incorporation of labeled fucose in either subunit. The effect of T3 on the rate constant of degradation of renal cortical Na+-K+-ATPase was assessed. The rate constant of degradation (Kd) of the [3H]fucose labeled alpha- and beta-subunits for the hypothyroid rats were both 0.20, and for T3-treated rats, the Kd of the alpha- and beta-subunits were 0.23 and 0.18, respectively, suggesting that T3 enhanced fucose incorporation into the subunits of Na+-K+-ATPase rather than retarding the degradation of this enzyme.

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