Single enzymes of E. coli sourced B-galactosidase were analysed in effort to expand the wealth of knowledge in the area of heterogeneity. Static and dynamic heterogeneity was studied with respect to catalytic rate, electrophoretic mobility, and heat shock protein chaperone systems. Temperature was found to be a contributing factor to the observed range of dynamic heterogeneity, with the range increasing with temperature. The inhibitor dissociation constant was determined to be a heterogeneous property of B-galactosidase. A novel assay was developed in which a single enzyme molecule was subjected to three separate solutions while the enzyme itself remained free in solution. / October 2016
| Identifer | oai:union.ndltd.org:MANITOBA/oai:mspace.lib.umanitoba.ca:1993/31769 |
| Date | January 2016 |
| Creators | Jeremie, Crawford |
| Contributors | Craig, Doug (Chemistry), McKenna, Sean (Chemistry) Perreault, Helene (Chemistry) Ayele, Belay (Plant Science) |
| Publisher | Biochemistry and Cell Biology, Electrophoresis |
| Source Sets | University of Manitoba Canada |
| Detected Language | English |
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