Free lysine, glycine, alanine, glutamic acid and aspartic acid reduce the glycation of human lens proteins by galactose

Indian J Biochem Biophys. 1997 Dec;34(6):518-23.


The amino acids lysine, glycine, alanine, glutamate and aspartate formed adducts with galactose at physiological pH and temperature as shown by incorporation of U[14C] galactose. The percentage of galactose reacting with lysine, glycine, alanine, glutamate and aspartate was 4.5 to 7.8, 7.9 to 10.8, 3.2 to 4.6, 2.8 to 4.8 and 3 to 5.2, respectively. Studies with lysine showed that the extent of glycation of the free amino acid increased with time. Incubation of lens homogenate with galactose, effected glycation of proteins. Addition of lysine in concentrations of 5 and 10 mM to equimolar concentrations of galactose decreased the glycation of lens proteins by 64% to 71%; glycine, alanine, glutamate and aspartate decreased glycation by 23 to 68%, 32 to 61%, 35 to 56% and 26 to 61% respectively. Under similar conditions, glycine reacts to a greater extent than lysine, alanine, glutamic and aspartic acids. However, lysine was more effective than glycine, alanine, aspartic and glutamic acids in decreasing glycation of lens proteins by galactose. The decrease of glycation with added lysine increased with time. In general increase of amino acid concentration rather than that of sugar augmented the decrease of glycation of lens proteins.

MeSH terms

  • Adult
  • Amino Acids / pharmacology*
  • Cataract / etiology
  • Crystallins / chemistry
  • Crystallins / drug effects*
  • Crystallins / metabolism*
  • Galactose / metabolism
  • Galactose / pharmacology
  • Glucose / metabolism
  • Glucose / pharmacology
  • Glycosylation
  • Humans
  • In Vitro Techniques
  • Lysine / pharmacology
  • Middle Aged


  • Amino Acids
  • Crystallins
  • Glucose
  • Lysine
  • Galactose