Catalase: Physical and chemical properties, mechanism of catalysis, and physiological role.

A Deisseroth, AL Dounce - Physiological reviews, 1970 - journals.physiology.org
A Deisseroth, AL Dounce
Physiological reviews, 1970journals.physiology.org
Catalase is ubiquitously present in mammalian and nonmammalian aerobic cells containing
a cytochrome system (86), and with a few exceptions (Acetobacter peroxydans and
ShigeZZa dysenteriae) only strict anaerobes lack this enzyme. Although catalase is present
in green plants, most workers have chosen to isolate the enzyme from bacterial and
mammalian sources where it is present in highest concentration, ie, Mic~ ococcus
Zysodeikticus, mammalian liver and erythrocytes, and occasionally kidney. Catalase is …
Catalase is ubiquitously present in mammalian and nonmammalian aerobic cells containing a cytochrome system (86), and with a few exceptions (Acetobacter peroxydans and ShigeZZa dysenteriae) only strict anaerobes lack this enzyme. Although catalase is present in green plants, most workers have chosen to isolate the enzyme from bacterial and mammalian sources where it is present in highest concentration, ie, Mic~ ococcus Zysodeikticus, mammalian liver and erythrocytes, and occasionally kidney. Catalase is primarily an intracellular enzyme, as confirmed by Agner (7) in the case of blood catalase. DeDuve and Baudhuin (43) have shown that catalase is present within liver cells in highest concentration in the microbodies. The history of the development of methods for the purification of catalase from liver and blood [reviewed by Sumner (142)] has been marked by the successful purification of a hemoglobin-free erythrocyte catalase by Wolff and de Stoecklin in 19 10 (160), the introduction of fractional denaturation of contaminating protein through alcoholic precipitation by Waentig and Gierisch in 1914 (159), the use of adsorption on an inert adsorbent by Hennichs (63) for concentration and purification, and the demonstration by Tsuchihashi in 1923 (156) that a mixture of ethanol and chloroform could be used to denature hemoglobin without denaturing catalase. All catalases are not, however, resistant to denaturation by chloroformethanol, as discussed later. The end of this early era, during which most work was
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