I just did a lab that measures the succinate dehydrogenase in mitochondria using an artificial electron acceptor.
We used both broken and intact mitochondria preparations, and I'm wondering what the significance in this is.
Thanks!
2007-03-05 16:22:42 · 2 answers · asked by Frannie 4 in Science & Mathematics ➔ Biology
Why did we use both broken mitochondria and intact mitochondria? I think it has something to do with the proteins that are membrane bound and not membrane bound.
2007-03-05 17:24:22 · update #1
Succinate dehydrogenase, which catalyzes succinate oxidation to fumarate, is the only enzyme in the tricarboxylic acids cycle that is not free in the mitochondrial matrix: it is an integral membrane protein.
i think it's just to increase the amount of succinate dehydrogenase in your solution since it is not free. it may also have something to do with the binding of the enzyme to known concentrations. im not so sure. you could have asked your teacher for the answer..
2007-03-05 18:09:18 · answer #1 · answered by mcsteamyandme 3 · 0⤊ 0⤋
I'm not understanding the qtion exactly
2007-03-05 17:07:19 · answer #2 · answered by Anonymous · 0⤊ 0⤋