Starch Gel Electrophoresis of Hen Egg White, Oviduct White, Yolk, Ova and Serum Proteins

Nature ◽  
1961 ◽  
Vol 192 (4806) ◽  
pp. 972-972 ◽  
Author(s):  
F. STEVEN
Keyword(s):  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Egg White ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Hen Egg White ◽  
Hen Egg

Starch-gel Electrophoresis of Pig Serum Proteins

Nature ◽  
1963 ◽  
Vol 197 (4873) ◽  
pp. 1201-1201 ◽  
Author(s):  
R. K. SCOPES
Keyword(s):  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Starch Gel Electrophoresis ◽  
Starch Gel ◽  
Pig Serum

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.

CHARACTERISTIC ELECTROPHORETIC PATTERNS OF SERUM PROTEINS OF SEVERAL SPECIES OF SNAKES OF IRAN

1965 ◽  
Vol 43 (4) ◽  
pp. 459-461 ◽  
Author(s):  
M. Latifi ◽  
K. D. Shamloo ◽  
A. Amin
Keyword(s):  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Starch Gel Electrophoresis ◽  
Gel Method ◽  
Electrophoretic Patterns ◽  
Starch Gel

Paper and starch-gel electrophoresis of serum proteins of several species and subspecies of poisonous and nonpoisonous snakes of Iran have been investigated. The patterns obtained, especially by means of the starch-gel method, are characteristic for each species. Electrophoretic patterns of samples of serum from different individuals of the same species were very similar.

scholarly journals Starch Gel Electrophoresis of Rat Serum Proteins

1961 ◽  
Vol 236 (7) ◽  
pp. 2005-2008
Author(s):  
George H. Beaton ◽  
Anne E. Selby ◽  
Margaret J. Veen ◽  
Audrey M. Wright
Keyword(s):  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Starch Gel Electrophoresis ◽  
Rat Serum ◽  
Starch Gel

Development of protein polymorphisms in redwing blackbirds

Development ◽  
1972 ◽  
Vol 28 (3) ◽  
pp. 481-489
Author(s):  
Alan H. Brush ◽  
Alan F. Scott
Keyword(s):  
Gel Electrophoresis ◽  
Tissue Specificity ◽  
Egg White ◽  
Agelaius Phoeniceus ◽  
Starch Gel Electrophoresis ◽  
Adult Tissue ◽  
Breeding Populations ◽  
Developmental Sequences ◽  
General Esterases ◽  
Starch Gel

Breeding populations of the redwing blackbird, Agelaius phoeniceus, were studied to compare protein differences during development. Proteins which represented a minimum of ten loci were studied in egg white, embryonic, nestling and adult tissue. In starch-gel electrophoresis at several conditions of pH only ovoglobulin, ovotransferrin and general esterases were polymorphic. Tissue specificity was observed in other isozymes. These data suggest that developmental sequences of proteins may be considered an adaptative response of the organism.

Thin-Layer Starch-Gel Electrophoresis

1966 ◽  
Vol 12 (9) ◽  
pp. 596-605 ◽  
Author(s):  
Lena A Lewis
Keyword(s):  
Thin Layer ◽  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Starch Gel Electrophoresis ◽  
Good Reproducibility ◽  
Starch Gel ◽  
Electrophoretic Fractionation

Abstract A modification of the starch-gel electrophoresis technic of Smithies is presented,which enables quantitation of the resolved fractions to be carried out with little equipment other than that used for paper electrophoretic fractionation of proteins.A sheet of plastic (Stabilene film) wrapped around a kymograph type drum is evenly coated with starch-gel. The sheet is suspended in an "open strip" Durrum type cell and electrophoresis carried out. After staining with suitable stain to demonstrate proteins, lipids, or other components, the patterns are scanned in a photoelectric densitometer. Results obtained with this procedure show good reproducibility when fractionating solutions of hemoglobin and serum proteins.

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