scholarly journals An apparatus for thin layer vertical polyacrylamide gel electrophoresis with discontinuous buffer system, and its practical applications

1974 ◽  
Vol 19 (2) ◽  
pp. 143-150
Author(s):  
Kunio Ariyoshi
2006 ◽  
Vol 27 (14) ◽  
pp. 2984-2995 ◽  
Author(s):  
Taufika Islam Williams ◽  
Jennifer C. Combs ◽  
Anup P. Thakur ◽  
Herbert J. Strobel ◽  
Bert C. Lynn

1973 ◽  
Vol 17 (2) ◽  
pp. 71-76
Author(s):  
Manabu Masuzawa ◽  
Takenobu Kamata ◽  
Yasuhiko Sakoyama ◽  
Yasuto Chiba ◽  
Zen-ichi Ogita

1974 ◽  
Vol 19 (2) ◽  
pp. 139-142
Author(s):  
Makoto Otsuki ◽  
Susumu Saeki ◽  
Hosai Yuu ◽  
Tsutomu Kondo ◽  
Shigeaki Baba

1977 ◽  
Author(s):  
K.J. Clemetson ◽  
S.L. Pfueller ◽  
A. Sturk ◽  
E.F. Lüscher ◽  
C.S.P. Jenkins

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.


1973 ◽  
Vol 133 (4) ◽  
pp. 655-665 ◽  
Author(s):  
Christopher H. S. McIntosh ◽  
David T. Plummer

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.


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