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. 2009 Mar 19;10(3):1314–1345. doi: 10.3390/ijms10031314

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© 2009 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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Figure 18. — Effect of α-crystallin on the kinetics of thermal inactivation of mAAT (0.1 mg/mL) at 65 °C (10 mM Na-phosphate buffer, pH 7.5). The dependences of the relative enzymatic activity (A/A₀) of mAAT. The concentrations of α-crystallin were as follows: (1) 0, (2) 0.05 and (3) 0.1 mg/mL.