Photosensibilisierte Oxidation von Lysozym bei Verschiedenen Wellenlängen

The photooxidation of lysozyme in the presence of methylene blue, riboflavine, and bengal rose at differentpH values and wavelengths was studied. Monochromatic irradiation at shorter wavelengths (345 and 365 nm) is - in contrast to visible light - characterized by higher energy yields and lower oxygen consumption. This behavior suggests that the mechanism of photooxidation depends on the wavelength. The specific destruction of amino acid residues is also wavelength-dependent. Using visible light of 448 and 621 nm for riboflavine and methylene blue, respectively, we have confirmed the selective destruction of histidine and tryptophan atpH 7,0. The energy yield for the destruction of tryptoph…

Microorganisms in the Space Environment

Preliminary results of the Spacelab 1 experiment on the response of Bacillus subtilis spores to conditions of free space are presented. Exposure to the vacuum of space on the Spacelab pallet reduced viability counts about 50 percent and increased mutation frequencies by a factor of about 10. Interpretation of apparent differences in the photobiological and photochemical data between flight and ground simulation experiments will require more statistical analyses and data from actual fluence measurements.

Simultaneous isolation of xanthomegnin, viomellein, rubrosulphin, viopurpurin, and brevianamide A by preparative HPLC.

A method for the isolation of xanthomegnin, viomellein, rubrosulphin, viopurpurin, and brevianamide A from Penicillium viridicatum (DSM 2447) is described. After extraction, HPLC was performed with a preparative silicagel column, eluted with toluene / ethyl acetate / formic acid (27/9/1, v/v/v) and dichloromethane / acetic acid (9/1, v/v). The toxins were detected with a UV-monitor. It was possible to isolate them in an absolutely pure state. The described method is operationally simple and very efficient.

Response of membrane-bound ATPase of Micrococcus luteus to heat and ultraviolet light.

It is shown that the properties of ATPase (EC 3.6.1.3) of Micrococcus luteus depend only to some extent on the state of the membrane to which it is attached. Its interaction with the membrane appears to be largely controlled by polar forces. It is shown, however, that the UV-sensitivity of the membrane-bound ATPase is also significantly influenced by the state of membrane lipids.

Vitamin K epoxide reductase activity in the metabolism of epoxides

Abstract The importance of vitamine K epoxide reductase for the metabolism of a range of structurally diverse epoxides has been investigated. Vitamin K 1 epoxide is reduced by rat liver microsomes at a rate of 0.47 nmoles/g liver/min. The rate of menadione oxide reduction is not significantly higher than the non-enzymatic reduction rate. No measurable reduction of benzo[ a ]pyrene 4,5-oxide, benzo[ a ]pyrene 7,8-oxide, phenanthrene 9,10-oxide, styrene 7,8-oxide, and dieldrin has been detected, nor could trichothecene T-2 toxin inhibit reduction of vitamin K 1 epoxide. Thus, vitamin K epoxide reductase is very specific for vitamin K 1 epoxide. Taking into account the range of structurally di…

Photochemically induced cross-links between DNA and alcohol dehydrogenase or salmine, respectively

Model experiments with two structurally different proteins (alcohol dehydrogenase and salmine) show that glycine, alanine, and tyrosine are by far more frequently involved in photochemically induced cross-link formations with DNA than is cysteine. The yields for cross-link formation of thymidine with salmine (cysteine-free) are about as high as those with alcohol dehydrogenase (a thiol protein).

Effects of photodynamic processes and ultraviolet light on duck and hen egg-white lysozymes.

— The photochemical yields for inactivation and amino acid destruction in hen and duck egg-white lysozyme are presented. Duck lysozyme II is devoid of histidine but it has two more tyrosine residues than does hen lysozyme. The data indicate that sensitized oxidation of the single histidine residue of hen lysozyme is of no significance for the inactivation of this lysozyme. The ultraviolet destruction of tryptophan and cystine residues appears to be equally related with the loss in enzymatic activity of hen lysozyme. In the case of duck lysozyme, however, the ultraviolet inactivation appears to be predominantly governed by the destruction of cystine residues.

Identification of acetyl-T-2 toxin, a trichothecene, in moldy rice by HPLC and FDMS