Arginase-less mutants

Dipicolinic acid-less mutants of Bacillus cereus.

When J. Powell (Biochem. J. 54:210, 1953) established dipicolinic acid (DPA) as an important constituent of bacterial spores, microbiologists became concerned about the function this compound serves and about its biosynthetic pathway. It is now generally considered that DPA is involved in the heat resistance of spores, but the mechanism is unknown. A number of schemes have been proposed for its...

Arginase and vascular aging.

Vascular and associated ventricular stiffness is one of the hallmarks of the aging cardiovascular system. Both an increase in reactive oxygen species production and a decrease in nitric oxide (NO) bioavailability contribute to the endothelial dysfunction that underlies this vascular stiffness, independent of other age-related vascular pathologies such as atherosclerosis. The activation/upregula...

Arginase status in bull reproductive system

The Activation of Arginase

The mechanism of arginase activation has been widely studied during the past few years. Salaskin and Solowjew (1) and Waldschmidt-Leitz, Schaffner, and Kocholaty (2) believed that sulfhydryl compounds were the specific activators of arginase. This viewpoint was attacked by Edlbacher, Kraus, and Walter (3), and by Klein and Ziese (4), who presented evidence that the effect obtained with sulfhydr...

Photooxidative stress stimulates illegitimate recombination and mutability in carotenoid-less mutants of Rubrivivax gelatinosus.

Carotenoids are essential to protection against photooxidative damage in photosynthetic and non-photosynthetic organisms. In a previous study, we reported the disruption of crtD and crtC carotenoid genes in the purple bacterium Rubrivivax gelatinosus, resulting in mutants that synthesized carotenoid intermediates. Here, carotenoid-less mutants have been constructed by disruption of the crtB gen...