PMID: 2493343Mar 1, 1989Paper

D-lysine effectively decreases the non-enzymic glycation of proteins in vitro

Clinical Chemistry
M SensiU Di Marlo

Abstract

Excessive non-enzymic glycation of proteins alters their physicochemical properties, with possible pathological effects. We investigated the in vitro inhibition of protein glycation by D-lysine--an isomer not incorporated into mammalian proteins but possessing the same chemical characteristics as L-lysine. Glucose incorporation was studied as follows: (a) human albumin, IgG, collagen, and isolated glomerular basement membrane were incubated for 20 days with D-glucose (5.0, 10.0, and 20.0 mmol/L) in the presence of D-lysine at 1/10 the sugar concentration; (b) albumin was incubated in similar glucose concentrations but with a constant amount (2.0 mmol/L) of D-lysine; (c) albumin and IgG were incubated for 10 days in buffer containing glucose (10 mmol/L) and increasing concentrations of D-lysine (0.25, 0.5, 1.0, 2.0, and 4.0 mmol/L); (d) inhibition specificity was tested by treating albumin as in c but with glycerol present rather than D-lysine. In addition, we measured ketoamine after incubating albumin (50 g/L) in 10 mmol/L glucose for 10 days in the presence of D-lysine (0.25, 0.5, 1.0, and 2.0 mmol/L). The results show that (a) the amount of glucose bound to the four proteins was significantly (P less than 0.05) decreased in ...Continue Reading

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