6533b862fe1ef96bd12c6d51
RESEARCH PRODUCT
Effects of photodynamic processes and ultraviolet light on duck and hen egg-white lysozymes.
S. RisiE. SilvaK. Dosesubject
LightPhotochemistryUltraviolet RaysCystineBiochemistrychemistry.chemical_compoundEgg WhiteSpecies SpecificityUltraviolet lightAnimalsPhysical and Theoretical ChemistryTyrosineAmino AcidsHistidinechemistry.chemical_classificationTryptophanGeneral MedicineAmino acidRadiation EffectsEnzymeDuckschemistryBiochemistryFemaleMuramidaseLysozymeChickensdescription
— 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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1973-12-01 | Photochemistry and photobiology |