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. Author manuscript; available in PMC: 2013 Jan 18.
Published in final edited form as: J Am Chem Soc. 2012 Jan 3;134(2):1172–1180. doi: 10.1021/ja209016j

Figure 2.

Figure 2

Purification and activity of α2 mutants. (a) SDS-PAGE of each mutant after purification indicates a monomer molecular weight at the expected retention (85 kD). (b) Quantification of the gel lanes in (a) by integrating the band density indicates that >98% of the protein in solution is α2 for each mutant prepared. (c) Activity of each enzyme quantified by counting turnover of [3H]-labeled CDP.