McLaughlin J A, Pethig R, Szent-Györgyi A
Proc Natl Acad Sci U S A. 1980 Feb;77(2):949-51. doi: 10.1073/pnas.77.2.949.
Spectroscopic measurements are reported for the effects of pH, time, solvent, and chemical modification of arginine and lysine side chains on the reaction of proteins with methylglyoxal. The reaction responsible for the appearance of a brown coloration and increased submolecular electronic activity in the proteins involves the epsilon-amino groups of the lysine residues. It is concluded that the primary step in the reaction involves the formation of a Schiff base linkage between the lysine side chain and methylglyoxal. These findings reaffirm the concept that, by the formation of Schiff bases, aldehydes can act as electron acceptors in charge transfer interactions with proteins.
报道了光谱测量结果，研究了pH值、时间、溶剂以及精氨酸和赖氨酸侧链的化学修饰对蛋白质与甲基乙二醛反应的影响。蛋白质中出现棕色以及亚分子电子活性增加的反应涉及赖氨酸残基的ε-氨基。得出的结论是，该反应的第一步涉及赖氨酸侧链与甲基乙二醛之间形成席夫碱连接。这些发现再次证实了这样一个概念，即醛类可通过形成席夫碱在与蛋白质的电荷转移相互作用中充当电子受体。
