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The research in my lab consists of three separate, but related,
topics as follows:
(1)
Isolation and characterization of cytochrome oxidase protein subunits
from mammalian mitochondria and two micro-organisms (Thermophilic
bacteria P53 and Thiobacillus ferrioxidans). Our goal
is to compare the common protein subunits and their individual functions.
The procedures to identify these subunits are by Elisa and Western
blot analyses using polyclonal and monoclonal antibodies previously
prepared against the mammalian species. So far, we have found that
the three largest subunits are common in all cytochrome oxidase
samples, while little information is known about the smaller subunits.
Our eventual aim is to understand the detailed enzyme mechanism
of this important terminal member of electron transport chain and
its contribution to energy transduction.
(2)
In related studies to the above, another project is to elucidate
the function of the mitochondrial ATPase inhibitor protein in relation
to malignant hepatoma, as well as animal tissues of various age
and artificially induced toxicity. Again, we are using Elisa and
Western blot techniques for this purpose. Recently, the gene of
this protein has been cloned in our laboratory by my former graduate
student. We are measuring the in vivo level of this protein under
various experimental conditions.
(3)
Finally, recently we have identified a cholesterol-binding protein
in the inter-membrane space between the two mitochondrial membranes
both from normal and tumor tissues, although with elevated amounts
in the latter. We believe that this protein may play a vital role
in cholesterol accumulation in the tumor mitochondria and, hence,
alters energy metabolism in the tumor tissue. There are a number
important biochemical characterization studies on this protein to
be done.
An
undergraduate student interested in such studies is particularly
welcome to join our laboratory.
Samuel Chan
310 BRL
443-3182
sachan@syr.edu |
