0000000000255690
AUTHOR
S. Risi
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…
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.
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.