Study of the Bacillus thuringiensis Vip3Aa16 histopathological effects and determination of its putative binding proteins in the midgut of Spodoptera littoralis

2011 ◽  
Vol 106 (2) ◽  
pp. 250-254 ◽  
Author(s):  
Lobna Abdelkefi-Mesrati ◽  
Hanen Boukedi ◽  
Mariam Dammak-Karray ◽  
Tahya Sellami-Boudawara ◽  
Samir Jaoua ◽  
...  
2013 ◽  
Vol 112 (2) ◽  
pp. 142-145 ◽  
Author(s):  
Dalel BenFarhat-Touzri ◽  
Marwa Saadaoui ◽  
Lobna Abdelkefi-Mesrati ◽  
Imen Saadaoui ◽  
Hichem Azzouz ◽  
...  

1970 ◽  
Vol 65 (1_Suppl) ◽  
pp. S104-S121 ◽  
Author(s):  
E. E. Baulieu ◽  
J. P. Raynaud ◽  
E. Milgrom

ABSTRACT A brief review of the characteristics of steroid binding proteins found in the plasma and in some target organs is presented, followed by some general remarks on binding »specificity« and binding parameters. Useful techniques for measuring binding parameters at equilibrium are reported, both those which keep the equilibrium intact and those which implicate its disruption. A concept is developed according to which the determination of a specific steroid binding protein is based on the »differential dissociation« of the several steroid binding complexes present in most biological mixtures. Methods which allow determination of the kinetic parameters of the binding systems are also presented. Various representations of the binding and therefore different modes of graphic representation and calculation are discussed, including the recent »proportion graph« method.


2005 ◽  
Vol 52 (1) ◽  
pp. 35-43 ◽  
Author(s):  
Agata Czyz ◽  
Grzegorz Wegrzyn

Members of the Obg subfamily of small GTP-binding proteins (called Obg, CgtA, ObgE or YhbZ in different bacterial species) have been found in various prokaryotic and eukaryotic organisms, ranging from bacteria to humans. Although serious changes in phenotypes are observed in mutant bacteria devoid of Obg or its homologues, specific roles of these GTP-binding proteins remain largely unknown. Recent genetic and biochemical studies, as well as determination of the structures of Obg proteins from Bacillus subtilis and Thermus thermophilus, shed new light on the possible functions of the members of the Obg subfamily and may constitute a starting point for the elucidation of their exact biological role.


1987 ◽  
Vol 22 (2-4) ◽  
pp. 235-248 ◽  
Author(s):  
J Pavičič ◽  
M Škreblin ◽  
B Raspor ◽  
M Branica ◽  
M Tušek-Ẑnidarič ◽  
...  

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