The myeloperoxidase system of human phagocytes generates N^ε-(carboxymethyl)lysine on proteins: a mechanism for producing advanced glycation end products at sites of inflammation
J. Clin. Invest. Melissa M. Anderson, et al. 104:103 doi:10.1172/JCI3042 [Go to this article.]

Figure 2
Fluorescence excitation and emission spectra of RNase A modified by HOCl-serine. RNase A (10 mg/mL) was modified for 24 hours at 37°C in buffer A with the HOCl-serine system at 10 mM each (a), as described in the legend to Figure 1; with 10 mM glycolaldehyde (b); or with 9 mM HOCl alone (c). Reaction mixture was then diluted 1:10 with 50 mM sodium citrate-citric acid buffer (pH 5.0), 50 mM sodium phosphate buffer (pH 7.0), or 50 mM boric acid-borax buffer (pH 9.0). The excitation and emission spectra of each reaction mixture were then determined. (d) Excitation and emission spectra of 1 mg/mL RNase A in 50 mM sodium phosphate buffer (pH 7.0).