scholarly journals The influence of magnesium ions and other bivalent metal ions on the aconitase equilibrium and its bearing on the binding of magnesium ions by citrate in rat heart

1967 ◽  
Vol 105 (2) ◽  
pp. 32C-33C ◽  
Author(s):  
P J England ◽  
R M Denton ◽  
P J Randle
Keyword(s):  
Metal Ions ◽  
Rat Heart ◽  
Magnesium Ions ◽  
Bivalent Metal ◽  
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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