Experimental probation on the binding kinetics and thermodynamics of Au(III) onto Bacillus subtilis

2011 ◽  
Vol 172 (1) ◽  
pp. 122-128 ◽  
Author(s):  
Yulan Ji ◽  
Hong Gao ◽  
Jinsheng Sun ◽  
Fang Cai
2007 ◽  
Vol 21 (5) ◽  
Author(s):  
JoDell Whittington ◽  
Torri Wood ◽  
Margaret Daugherty ◽  
Laura Parkhurst ◽  
Lawrence Parkhurst

2000 ◽  
Vol 39 (26) ◽  
pp. 5884-5894 ◽  
Author(s):  
Hong-Chang Liang ◽  
Kenneth D. Karlin ◽  
Raylene Dyson ◽  
Susan Kaderli ◽  
Bernhard Jung ◽  
...  

Author(s):  
Dwight Anderson ◽  
Charlene Peterson ◽  
Gursaran Notani ◽  
Bernard Reilly

The protein product of cistron 3 of Bacillus subtilis bacteriophage Ø29 is essential for viral DNA synthesis and is covalently bound to the 5’-termini of the Ø29 DNA. When the DNA-protein complex is cleaved with a restriction endonuclease, the protein is bound to the two terminal fragments. The 28,000 dalton protein can be visualized by electron microscopy as a small dot and often is seen only when two ends are in apposition as in multimers or in glutaraldehyde-fixed aggregates. We sought to improve the visibility of these small proteins by use of antibody labeling.


Sign in / Sign up

Export Citation Format

Share Document