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. Author manuscript; available in PMC: 2012 May 15.

Published in final edited form as: Free Radic Biol Med. 2011 Feb 23;50(10):1429–1436. doi: 10.1016/j.freeradbiomed.2011.01.036

Fig. 4 — Mass spectra of 10μM of mini-αA-crystallin in 5 mM of ammonium acetate buffer pH 6.3, with and without Cu²⁺. A) mini-αA without Cu²⁺; B) + 2 μM Cu²⁺; C) + 5 μM Cu²⁺; D) + 10 μM Cu²⁺ and E) + 20 μM Cu²⁺.

F) Estimation of peptide-Cu²⁺ complex concentrations after mass spectrometric analysis. 1) amount of one Cu²⁺ –mini-αA-crystallin complex; 2) free mini-αA-crystallin and 3) two Cu²⁺ –mini-αA complex.

G) The binding of Cu²⁺ ions to 10 μM of mini-αA-crystallin at pH 6.3 as a function of the concentration of total Cu²⁺ added. K_D= 5.1 μM can be derived from the half-maximal value in curve.

Fig. 4 — Mass spectra of 10μM of mini-αA-crystallin in 5 mM of ammonium acetate buffer pH 6.3, with and without Cu²⁺. A) mini-αA without Cu²⁺; B) + 2 μM Cu²⁺; C) + 5 μM Cu²⁺; D) + 10 μM Cu²⁺ and E) + 20 μM Cu²⁺.

F) Estimation of peptide-Cu²⁺ complex concentrations after mass spectrometric analysis. 1) amount of one Cu²⁺ –mini-αA-crystallin complex; 2) free mini-αA-crystallin and 3) two Cu²⁺ –mini-αA complex.

G) The binding of Cu²⁺ ions to 10 μM of mini-αA-crystallin at pH 6.3 as a function of the concentration of total Cu²⁺ added. K_D= 5.1 μM can be derived from the half-maximal value in curve.