scholarly journals Comparative Study of Uptake and Cellular Distribution of Hg203-Labeled Phenyl-Mercuric Acetate and Mercuric Acetate by Pea Roots

1966 ◽  
Vol 41 (3) ◽  
pp. 443-446 ◽  
Author(s):  
A. V. Rao ◽  
Elizabeth Fallin ◽  
S. C. Fang
1973 ◽  
Vol 21 (12) ◽  
pp. 2695-2704 ◽  
Author(s):  
TOZO FUJII ◽  
SHIGEYUKI YOSHIFUJI ◽  
KAZUHIKO MICHISHITA ◽  
MORIHIRO MITSUKUCHI ◽  
KIYOSHI YOSHIDA

2020 ◽  
Author(s):  
Bruno Oliveira Ferreira de Souza ◽  
Éve‐Marie Frigon ◽  
Robert Tremblay‐Laliberté ◽  
Christian Casanova ◽  
Denis Boire

Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.


2001 ◽  
Vol 268 (6) ◽  
pp. 1739-1748
Author(s):  
Aitor Hierro ◽  
Jesus M. Arizmendi ◽  
Javier De Las Rivas ◽  
M. Angeles Urbaneja ◽  
Adelina Prado ◽  
...  

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