scholarly journals Purification and characterization of a carboxypeptidase-transpeptidase of Bacillus megaterium acting on the tetrapeptide moiety of the peptidoglycan.

1979 ◽  
Vol 254 (13) ◽  
pp. 5672-5683
Author(s):  
H DasGupta ◽  
D P Fan
Keyword(s):  
Bacillus Megaterium ◽  
Purification And Characterization

The purification and characterization of a DNA nicking–closing enzyme from Bacillus megaterium

1978 ◽  
Vol 56 (2) ◽  
pp. 123-128 ◽  
Author(s):  
M. G. Burrington ◽  
A. Richard Morgan
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Bacillus Megaterium ◽  
Enzyme Preparation ◽  
Micrococcus Luteus ◽  
Purification And Characterization ◽  
Dna Nicking ◽  
Negative Supercoils

Although several eucaryote DNA nicking–closing (N–C) enzymes have been characterized, only the Escherichia coli enzyme has been extensively studied amongst procaryotes. The latter enzyme is distinctly different from the eucaryotic enzymes and we have therefore purified the N–C enzyme from Bacillus megaterium to determine if procaryotes form a distinctive class of N–C enzymes. The purified B. megaterium N–C enzyme has a molecular weight of 120 000, only partly relaxes negative supercoils, does not affect positive supercoils, requires Mg2+, and is inhibited by 0.2 M KCl. The enzyme is also inhibited by 1 mM nalidixic or oxolinic acids but unaffected by novobiocin. A crude N–C enzyme preparation from Micrococcus luteus shows very similar properties.

Purification and characterization of a protease produced by Bacillus megaterium RRM2: application in detergent and dehairing industries

2011 ◽  
Vol 51 (6) ◽  
pp. 614-624 ◽  
Author(s):  
Renganathan Rajkumar ◽  
Kothilmozhian Ranishree Jayappriyan ◽  
Ramasamy Rengasamy
Keyword(s):  
Bacillus Megaterium ◽  
Purification And Characterization
Sign in / Sign up

Export Citation Format

Share Document