Information on DNA conformation derived from the Ferguson plot of DNA fragments of up to 9 kb in size, using polyacrylamide gel electrophoresis in a discontinuous buffer system

1991 ◽  
Vol 12 (4) ◽  
pp. 241-246 ◽  
Author(s):  
László Orbán ◽  
Andreas Chrambach
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Dna Conformation ◽  
Buffer System ◽  
Dna Fragments

A novel Bicine running buffer system for doubled sodium dodecyl sulfate – polyacrylamide gel electrophoresis of membrane proteins

2006 ◽  
Vol 27 (14) ◽  
pp. 2984-2995 ◽  
Author(s):  
Taufika Islam Williams ◽  
Jennifer C. Combs ◽  
Anup P. Thakur ◽  
Herbert J. Strobel ◽  
Bert C. Lynn
Keyword(s):  
Membrane Proteins ◽  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Buffer System ◽  
Dodecyl Sulfate

scholarly journals Isolation of Some Platelet Membrane Glycoproteins

1977 ◽  
Author(s):  
K.J. Clemetson ◽  
S.L. Pfueller ◽  
A. Sturk ◽  
E.F. Lüscher ◽  
C.S.P. Jenkins
Keyword(s):  
Gel Electrophoresis ◽  
Wheat Germ ◽  
Lens Culinaris ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Platelet Membrane ◽  
Buffer System ◽  
Membrane Glycoproteins ◽  
Abrus Precatorius ◽  
Differential Binding

The platelet is surrounded by a pronounced glycocalix formed by carbohydrate moieties of the membrane glycoproteins. The number of glycoproteins of the outer platelet membrane is greater in number than had previously been reported : when solubilized membranes are analyzed by SDS-polyacrylamide gel electrophoresis the number of separated carbohydrate entities was found not only to be dependant on the concentration of acrylamide and of bisacrylamide used but also on the buffer system employed.The major platelet membrane glycoproteins have been solubilized and subjected to affinity chromatography on the lectins from Lens culinaris, wheat germ and Abrus precatorius. SDS-polyacrylamide gel electrophoresis in the presence and absence of a reducing agent together with the differential binding of the lectins to the glycoproteins permitted the distinction of at least seven glycoprotein entities. Using combinations of lectin columns, two platelet membrane glycoproteins have been isolated and others have been greatly purified.

scholarly journals Multiple forms of acetylcholinesterase from pig brain

1973 ◽  
Vol 133 (4) ◽  
pp. 655-665 ◽  
Author(s):  
Christopher H. S. McIntosh ◽  
David T. Plummer
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Buffer System ◽  
Soluble Enzyme ◽  
Molecular Weights ◽  
Pig Brain ◽  
Spacer Gel ◽  
Solubilized Enzyme ◽  
Triton X

1. A number of methods of solubilization of pig brain acetylcholinesterase (EC 3.1.1.7) were studied. The multiple enzymic forms of the resultant preparations were examined by polyacrylamide-gel electrophoresis. 2. Butanol extraction, Nagarase treatment and ultrasonication proved unsuitable as preparatory methods, but detergent treatment (Triton X-100, Triton X-100–KCl and lysolecithin) gave good yields. 3. Separation of soluble enzyme in three systems of polyacrylamide-gel electrophoresis were compared and the relative advantages are discussed. 4. By using a 6% (w/v) gel and continuous buffer system two forms of acetylcholinesterase were detected in Triton X-100-solubilized enzyme, but the incorporation of a sample and spacer gel and a discontinuous buffer system resolved this into four components. The forms of the soluble enzyme extracted by different methods differed in mobility. 5. With gradient polyacrylamide-gel electrophoresis between two and six forms were detected, depending on the method used for extraction. The average molecular weights of the five forms most frequently found were 60000, 130000, 198000, 266000 and 350000. 6. Treatment of the Triton X-100-extracted enzyme with 2.5m-urea altered the pattern and evidence of dissociation was observed. 7. The results are discussed in the light of present theories on the molecular structure of acetylcholinesterase.

Horizontal polyacrylamide gel electrophoresis for the separation of DNA fragments

1994 ◽  
Vol 15 (1) ◽  
pp. 153-158 ◽  
Author(s):  
Hildegard Haas ◽  
Bruce Budowle ◽  
Günter Weiler
Keyword(s):  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Dna Fragments

scholarly journals Dodecyl sulphate/polyacrylamide-gel electrophoresis at low pH values and low temperatures

1979 ◽  
Vol 181 (3) ◽  
pp. 759-761 ◽  
Author(s):  
R Lichtner ◽  
H U Wolf
Keyword(s):  
Low Temperatures ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Catalyst System ◽  
Low Ph ◽  
Polyacrylamide Gel ◽  
Buffer System ◽  
Simple Method ◽  
Ph Values

A simple method is described for dodecyl sulphate/polyacrylamide-gel electrophoresis of pH- and temperature-labile biological intermediates. The method is based on a catalyst system that works at temperatures of 2–4 degrees C and pH values of 2–4 and an appropriate buffer system containing Li+ or Tris [CH2OH–C(CH2OH)2–NH3+] instead of Na+. This system does not lead to the precipitation of 1% dodecyl sulphate.

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