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Our laboratory is interested in the organization of metabolism. It has
evidence that intermediates in glycolysis and in the oxidative limb of the
pentose phosphate pathway are "channeled" from one enzyme to the next
rather than dissociating as product after the first catalytic event and
equilibrating with like molecules in the bulk medium. Such a mode of
functioning is consistent with the interaction of pathway enzymes, and has
profound consequences for the manner in which the cell functions. The lab
is developing a system that will allow the investigator to make
quantitative estimates of the degree of channeling in in vivo
systems.
The second activity in our lab aims at associating known enzymatic
activities with their previously unknown genes. The most usual approach to
associating genes and the activity of their products involves monitoring
changes in gene expression in response to changed environmental
conditions, e.g., salt stress. Using 2-D gel electrophoresis and mass
spectrometry data, along with the associated software, genes for the
proteins whose expression level changes are identified. But the activity
of the protein remains unknown. By contrast, we start with the known
activity, partially purify the protein that gives rise to the activity and
correlate the increase in the amount of protein at each purification step
with the increase in the specific activity of the protein.
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