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Single amino acid substitutions of alpha 1-antitrypsin that confer enhancement in thermal stability
Journal of Biological Chemistry
A recombinant alpha 1-antitrypsin variant which increased thermal stability was obtained from random mutagenesis followed by screening. The clone was identified as having a single mutation of Phe51-->Cys. Heat deactivation of purified recombinant alpha 1-antitrypsin produced in Escherichia coli revealed that the mutation slowed down the deactivation rate 10-fold at 57 degrees C, increasing thermal stability of recombinant protein to almost that of natural glycosylated plasma form. The mutantpmid:8144550 fatcat:tdukwgd63ncorjjun6ean3ehuq