Purification and biochemical characterization of a novel carbonic anhydrase II from erythrocytes of camel (Camelusdromedarius).

A novel carbonic anhydrase II (CA II) from erythrocytes of camel (Camelus dromedarius) was purified to homogeneity using affinity chromatography and biochemically characterized. Specific activity of 140.88 U/mg was obtained with 745.

Purification and biochemical characterization of catalase that confers protection against hydrogen peroxide induced by stressful desert environment: the kidney catalase.

Camel is continually exposed to stressful desert environment that enhances generation of reactive oxygen species, including hydrogen peroxide (HO). Catalase plays an important role in detoxification of HO. A highly active catalase from camel kidney was purified to homogeneity, with a specific activity of 1,774,392 U/mg protein, using ion exchange and metal chelate affinity chromatography.

Sulfanilamide Modified Magnetic Nanoparticles for Purification of Carbonic Anhydrase from Bovine Blood.

Magnetic nanoparticles (MNPs) have been used for purification of specific biomolecules form mixtures. The aim of this study is to develop a new, cheap, reusable, and magnetic-based material to purify the carbonic anhydrase (CA) enzyme in a short time with high efficiency. In the first part of this study, silica-coated iron oxide magnetic nanoparticles (FeO@SiO MNPs) were obtained.

A novel acid phosphatase from cactus (Opuntia megacantha Salm-Dyck) cladodes: Purification and biochemical characterization of the enzyme.

Acid phosphatase (ACP) plays an important role in regulating phosphate nutrition in plants. Herein, for the first time, a novel ACP from Opuntia megacantha Salm-Dyck cladodes was purified to homogeneity and biochemically characterized. Specific activity of 8.

Purification and biochemical characterization of a novel copper, zinc superoxide dismutase from liver of camel (Camelus dromedarius): An antioxidant enzyme with unique properties.

A novel copper, zinc superoxide dismutase (CuZnSOD) was purified to homogeneity from the liver of an animal well adapted to the stressful living conditions of the desert, the camel (Camelus dromedarius). The biochemical properties of camel liver CuZnSOD were examined. The purified enzyme had a native molecular weight of 28 kDa, as judged by gel filtration chromatography, and showed a single band at 27 kDa on SDS-PAGE, indicating that it is a monomeric protein.

Purification of camel liver catalase by zinc chelate affinity chromatography and pH gradient elution: An enzyme with interesting properties.

Climate change and increasing temperatures are global concerns. Camel (Camelus dromedarius) lives most of its life under high environmental stress in the desert and represent ideal model for studying desert adaptation among mammals. Catalase plays a key role in protecting cells against oxidative stress.