Elimination of hydrogen peroxide by Haemophilus somnus, a catalase-negative pathogen of cattle

Homocysteine Inhibits Hydrogen Peroxide Breakdown by Catalase

Catalase, an antioxidant enzyme responsible for degradation of hydrogen peroxide, is protective in many diseases. The amino-acid homocysteine has been suggested to be a pro-oxidant with elevated levels linked to the oxidative stress seen in Alzheimer’s and other diseases. This study shows that homocysteine inhibits the breakdown of hydrogen peroxide by catalase. Physiological concentrations of ...

Membrane Protein of Haemophilus somnus

We purified the major outer membrane protein (MOMP), which is the most abundant OMP (with an apparent molecular mass of 40 kDa), from Haemophilus somnus strain 8025. The method involves solubilization of the MOMP with Zwittergent 3-14 and further purification accomplished by ion-exchange and molecular-sieve chromatographies. The amino-terminal sequence of the MOMP showed considerable similarity...

Studies on the Inactivation of Catalase Iii. Destruction of Catalase by Hydrogen Peroxide by Sergius Morgulis

Hydrogen peroxide homeostasis: activation of plant catalase by calcium/calmodulin.

Environmental stimuli such as UV, pathogen attack, and gravity can induce rapid changes in hydrogen peroxide (H(2)O(2)) levels, leading to a variety of physiological responses in plants. Catalase, which is involved in the degradation of H(2)O(2) into water and oxygen, is the major H(2)O(2)-scavenging enzyme in all aerobic organisms. A close interaction exists between intracellular H(2)O(2) and ...

The Decomposition of Hydrogen Peroxide by Liver Catalase

1. The velocity of decomposition of hydrogen peroxide by catalase as a function of (a) concentration of catalase, (b) concentration of hydrogen peroxide, (c) hydrogen ion concentration, (d) temperature has been studied in an attempt to correlate these variables as far as possible. It is concluded that the reaction involves primarily adsorption of hydrogen peroxide at the catalase surface. 2. Th...