Journal
BIOCHEMISTRY
Volume 42, Issue 6, Pages 1707-1710Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi0204138
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- NIGMS NIH HHS [GM20066] Funding Source: Medline
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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).
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