Biochemistry (Washington) 2003-02-18

Crystallization of beta-galactosidase does not reduce the range of activity of individual molecules.

Glen K Shoemaker, Douglas H Juers, Jennifer M L Coombs, Brian W Matthews, Douglas B Craig

文献索引：Biochemistry 42(6) , 1707-10, (2003)

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摘要

By use of a capillary electrophoresis-based procedure, it is possible to measure the activity of individual molecules of beta-galactosidase. Molecules from the crystallized enzyme as well as the original enzyme preparation used to grow the crystals both displayed a range of activity of 20-fold or greater. beta-Galactosidase molecules obtained from two different crystals had indistinguishable activity distributions of 31,600 +/- 1100 and 31,800 +/- 1100 reactions min(-1) (enzyme molecule)(-1). This activity was found to be significantly different from that of the enzyme used to grow the crystals, which showed an activity distribution of 38,500 +/- 900 reactions min(-1) (enzyme molecule)(-1).