An evaluation of the rate constants for the adsorption of the defective phage PBS Z to Bacillus subtilis

1982 ◽  
Vol 48 (2) ◽  
pp. 183-188 ◽  
Author(s):  
H. Y. Steensma
2003 ◽  
Vol 66 (8) ◽  
pp. 1482-1485 ◽  
Author(s):  
JUN SAWAI ◽  
HIROYUKI MIYOSHI ◽  
HIROMITSU KOJIMA

Scallop shell powder heated at 1,000°C for 1 h exhibited sporicidal action against Bacillus subtilis spores. The sporicidal kinetics of this action were analyzed with the use of a nonlogarithmic model. Apparent death rate constants (k) were obtained under various conditions. The value of k increased with powder concentration but became constant beyond the concentration representing the solubility of Ca(OH)2. A linear inverse relationship between k and temperature was found, and from this relationship the activation energy required for the death of B. subtilis spores in the heated shell powder slurry could be determined.


1968 ◽  
Vol 35 (3) ◽  
pp. 423-428 ◽  
Author(s):  
P. Swartling ◽  
B. Lindgren

SummaryAn investigation was made of the death-rate ofBacillus subtilisspores in suspension in hydrogen peroxide concentrations of 10, 15 and 20% at 25, 50, 60, 70 and 80°C. Average logarithmic survival curves were plotted against normal time and death-rate constants andQ10values were calculated from the graphically determined decimal reduction times. This treatment of the experimental findings was found to be warranted in the temperature range 60–80°C. The first-order death-rate constant was ∽ 0·1 s−1for 10% hydrogen peroxide solution at 60°C and theQ10was about 1·6. Increases in the concentration from 10 to 15% and from 15 to 20% each gave an increase of about 50% in the rate constant. The application of these data to commercial practice is discussed.


1968 ◽  
Vol 34 (3) ◽  
pp. 413-428 ◽  
Author(s):  
Koji Okamoto ◽  
J.A. Mudd ◽  
J. Mangan ◽  
W.M. Huang ◽  
T.V. Subbaiah ◽  
...  

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.


Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
N Padilla-Montaño ◽  
IL Bazzocchi ◽  
L Moujir

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