scholarly journals Analysis of water-soluble protein composition of fresh water snails, Indoplanorbis exustus, I. corneas and Biomphalaria glabrata, using two dimensional gel electrophoresis.

1986 ◽  
Vol 30 (6) ◽  
pp. 449-456
Author(s):  
Nobuhiro Nyumura ◽  
Hiroaki Asaga ◽  
Tsutomu Inoue
1982 ◽  
Vol 92 (2) ◽  
pp. 283-288 ◽  
Author(s):  
F D Howard ◽  
H R Petty ◽  
H M McConnell

Two-dimensional PAGE (P. Z. O'Farrell, H. M. Goodman, and P. H. O'Farrell. 1977. Cell. 12:1133-1142) has been employed to assess the effects of antibody-dependent phagocytosis on the cell surface protein composition of RAW264 macrophages. Unilamellar phospholipid vesicles containing 1% dinitrophenyl-aminocaproyl-phosphatidylethanolamine (DNP-cap-PE) were used as the target particle. Macrophages were exposed to anti-DNP antibody alone, vesicles alone, or vesicles in the presence of antibody for 1 h at 37 degrees C. Cell surface proteins were then labeled by lactoperoxidase-catalyzed radioiodination at 4 degrees C. After detergent solubilization, membrane proteins were analyzed by two-dimensional gel electrophoresis. The resulting pattern of spots was compared to that of standard proteins. We have identified several surface proteins, not apparently associated with the phagocytic process, which are present either in a multichain structure or in several discretely charged forms. After phagocytosis, we have observed the appearance of two proteins of 45 and 50 kdaltons in nonreducing gels. In addition, we have noted the disappearance of a 140-kdalton protein in gels run under reducing conditions. These alterations would not be detected in the conventional one-dimensional gel electrophoresis. This evidence shows that phagocytosis leads to a modification of cell surface protein composition. Our results support the concept of specific enrichment and depletion of membrane components during antibody-dependent phagocytosis.


1984 ◽  
Vol 11 (1) ◽  
pp. 1-3 ◽  
Author(s):  
Sheikh M. Basha ◽  
Sunil K. Pancholy

Abstract Methionine-rich proteins (MRP) from seeds of different species of the Genus Arachis were isolated and analyzed by gel electrophoresis to detect possible compositional differences. One-dimensional gel electrophoretic analysis showed presence of quantitative and qualitative variations among the MRP-fractions. Following two-dimensional gel electrophoresis, the MRP-fractions were found to contain three groups of polypeptides with apparent molecular weights of approximately 21,000; 19,000 and 16,000, and isoelectric points between 5.1 and 5.8. Within each molecular weight group the number of polypeptides varied between 1 and 3.


1998 ◽  
Vol 46 (10) ◽  
pp. 3991-3997 ◽  
Author(s):  
C. Piñeiro ◽  
J. Barros-Velázquez ◽  
C. G. Sotelo ◽  
R. I. Pérez-Martín ◽  
J. M. Gallardo

2014 ◽  
Vol 1 (1) ◽  
Author(s):  
Sébastien Charneau ◽  
Gabriel Costa Nunes da Cruz ◽  
Camila Miranda Costa ◽  
Marcelo Valle de Sousa ◽  
Carlos André Ornelas

AbstractHigh-resolution separation by two-dimensional gel electrophoresis (2- DE) is still challenging due to the intrinsic behavior of proteins, principally throughout isoelectric focusing separation. It is often observed low resolution of proteins in the alkaline pH region when using wide range pH gradients. Herein, we show the effect of different concentrations of Triton X‑100 and DTT in the sample buffer on wide range pH (3-10) 2-DE profiles of three different biological samples as Trypanosoma cruzi cells, honey bee brain tissue and human saliva fluid. Higher resolution, number and intensity of spots were achieved when 85 mM DTT and 2.5% Triton X‑100 were employed for cell and tissue samples. No improvement was observed for fluid proteins, probably because water-soluble proteins do not require special conditions for extraction and prevention of precipitation during isoelectric focusing.


1994 ◽  
Vol 15 (suppl D) ◽  
pp. 37-44 ◽  
Author(s):  
M. Knecht ◽  
V. Regitz-Zagrosek ◽  
K.-P. Pleissner ◽  
P. Jungblut ◽  
C. Steffen ◽  
...  

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