The cofactor pyridoxal 5’-phosphate bound through an aldimine linkage to lysine residues of the enzyme aspartate amiuotransferase is very stable to irradiation with light of 420 nm. The catalytic function of the enzyme exposed to light absorbed by the cofactor remains unaffected, indicating that pyridoxal 5’-phosphate is not an efficient active site photosensitizer for this aminotransferase. Th...

Objectives: Antibiotics is the most common treatment for bacterial infections. However, bacteria can change their genetic material, develop antibiotic resistance and cannot be treated. This brings need new methods. Antibacterial Photodynamic Therapy becoming a promising approach to treat It based on use of photosensitizer activated by light with an appropriate wavelength it will result in react...

Photodynamic action/Acridine orange/tRNA/Guanine/Singlet oxygen The photodynamic inactivation of acridine orange (AO)-sensitized tRNA was investigated with respect to the type of photochemical pathways and the base damage leading to the inactivation. The diagnostic tests for singlet oxygen (1O2), namely the enhancement effect of deuterium oxide (D2O) and the inhibition effect by sodium azide, i...

In this study, the photoinactivation of Legionella by visible light is investigated. The success of this approach would offer new prospects for technical water disinfection and maybe even for therapeutic measures in cases of Legionella infections. Therefore, Legionella rubrilucens was dispensed on buffered charcoal yeast extract medium agar plates and illuminated with different doses of violet ...

Severe photoinactivation of catalase (EC 1.11.1.6) and a decline of variable fluorescence (F(v)), indicating photoinhibition of photosynthesis, were observed as rapid and specific symptoms in leaves exposed to a high heat-shock temperature of 40 degrees C as well as in leaves exposed to low chilling temperatures in white light of only moderately high photosynthetic photon flux density of 520 mu...

Isoelectric focusing was used as the final step in the isolation of thymidine phosphorylase which was found to have an isoelectric point of 4.1. Analytical acrylamide gel electrophoresis showed the purified enzyme preparation contained one major protein band which stained for thymidine phosphorylase activity and usually a minor, faster migrating band devoid of activity. Inactivation of thymidin...