Ferrer I, Silva E
Radiat Environ Biophys. 1985;24(1):63-70. doi: 10.1007/BF01212654.
Irradiation of lysozyme in the presence of riboflavin results in the formation of a lysozyme-riboflavin adduct. Reduction and carboxymethylation of the four disulfide bonds as well as the chemical modification of the Tyr residues and the photochemical alteration of the His residue in lysozyme, do not affect the formation of the photo-induced lysozyme-riboflavin bond. When the lysozyme-riboflavin adduct was subjected to mild acid hydrolysis and ion exchange chromatography, the retention of a compound containing 14C-riboflavin was observed. Free 14C-riboflavin, on the contrary is not retained by the column. The photo-oxidation of free Trp in the presence of 14C-riboflavin, gave a compound which bound to the ion exchange resin like the above-mentioned derivative. The photo-oxidation of the Trp residues in lysozyme and in peptides obtained from lysozyme showed very high quantum yields, and these values were directly related to the incorporation of 14C-riboflavin in these samples.
在核黄素存在的情况下对溶菌酶进行辐照会导致形成溶菌酶 - 核黄素加合物。对溶菌酶中的四个二硫键进行还原和羧甲基化，以及对酪氨酸残基进行化学修饰和对组氨酸残基进行光化学改变，均不影响光诱导的溶菌酶 - 核黄素键的形成。当溶菌酶 - 核黄素加合物进行温和酸水解和离子交换色谱分析时，观察到保留了一种含有¹⁴C - 核黄素的化合物。相反，游离的¹⁴C - 核黄素不被该柱保留。在¹⁴C - 核黄素存在下对游离色氨酸进行光氧化，得到一种与上述衍生物一样能与离子交换树脂结合的化合物。溶菌酶及其从溶菌酶获得的肽中色氨酸残基的光氧化显示出非常高的量子产率，并且这些值与¹⁴C - 核黄素在这些样品中的掺入直接相关。
