Hipkiss A R, Michaelis J, Syrris P
Division of Biomolecular Engineering, CSIRO, North Ryde, NSW, Australia.
FEBS Lett. 1995 Aug 28;371(1):81-5. doi: 10.1016/0014-5793(95)00849-5.
The dipeptide carnosine (beta-alanyl-L-histidine) was readily glycosylated non-enzymatically upon incubation with the sugars glucose, galactose, deoxyribose and the triose dihydroxyacetone. Carnosine inhibited glycation of actyl-Lys-His-amide by dihydroxyacetone and it protected alpha-crystallin, superoxide dismutase and catalise against glycation and cross-linking mediated by ribose, deoxyribose, dihydroxyacetone, dihydroxyacetone phosphate and fructose. Unlike certain glycated amino acids, glycated carnosine was non-mutagenic. The potential biological and therapeutic significance of these observations are discussed.
二肽肌肽（β-丙氨酰-L-组氨酸）在与葡萄糖、半乳糖、脱氧核糖和丙糖二羟基丙酮一起孵育时很容易发生非酶糖基化。肌肽抑制二羟基丙酮对乙酰-L-赖氨酸-组氨酸酰胺的糖基化作用，并且它能保护α-晶状体蛋白、超氧化物歧化酶和过氧化氢酶免受核糖、脱氧核糖、二羟基丙酮、磷酸二羟基丙酮和果糖介导的糖基化和交联作用。与某些糖基化氨基酸不同，糖基化肌肽没有致突变性。讨论了这些观察结果潜在的生物学和治疗意义。
