Studies on the interaction of antibiotic drug rifampin with DNA and influence of bivalent metal ions on binding affinity

2019 ◽  
Vol 219 ◽  
pp. 195-201 ◽  
Author(s):  
Nahid Shahabadi ◽  
Farshad Shiri ◽  
Saba Hadidi
Keyword(s):  
Metal Ions ◽  
Binding Affinity ◽  
Bivalent Metal ◽  
Antibiotic Drug ◽  
Bivalent Metal Ions

scholarly journals Separation and properties of two arylamidases from rat cardiac-muscle extracts

1977 ◽  
Vol 163 (3) ◽  
pp. 565-570 ◽  
Author(s):  
A F Bury ◽  
T Coolbear ◽  
C R Savery
Keyword(s):  
Metal Ions ◽  
Cardiac Muscle ◽  
Rat Heart ◽  
Bivalent Metal ◽  
Ph Optimum ◽  
Minor Peak ◽  
Bivalent Metal Ions ◽  
Stimulation Of

Two main arylamidase activities were separated from a particle-free supernatant of rat heart by chromatography on DEAE-Sephadex. Although both enzymes hydrolysed L-leucine 4-nitroanilide, only peak-II enzyme hydrolysed L-lysine 4-nitroanilide. A third minor peak (Ia) contained an enzyme that was active mainly on the L-lysine 4-nitroanilide. The mol.wts. of the enzymes in peaks I and II were approx. 257000 and 105000 respectively. The pH optimum was approx. pH7.0 for peak-I enzyme and 7.0-8.0 for peak-II enzyme. Both enzymes were inhibited by addition of puromycin, p-hydroxymercuribenzoate, o-phenanthroline and bivalent metal ions. Addition of dithiothreitol resulted in stimulation of both activities. Dialysis against o-phenanthroline resulted in inhibition of peak-I and -II enzymes, but after dialysis against EDTA only peak-II enzyme was inhibited.

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