Some challenges or surprises that we encountered was in
our hypothesis of what we thought would happen during our testing. We thought
that there would be a difference in the proteins from a leg meat (dark slow
twitch muscle) to a breast meat (white fast twitch muscle) from a turkey and a
chicken then the duck has both dark meat in the leg and Brest. When we ran the
gel electrophoresis we discovered there is no difference in the protein in the different
muscles. That kind of confused and surprised us so we ran the second gel and
sure enough the same thing happened. Then we sat down and thought about it some
more and we realized that we missed a key fact to why the muscles are different
between the fast and slow twitch, it’s because the darker meat has more
myoglobin which stores oxygen for are needed for long use of activity in the
muscle. This was not what we originally thought we thought that the proteins
that make up the muscle must be different but it’s just the build op of
myoglobin in the muscles that give them there fast and slow twitch
characteristics.
In our error analysis section of our discussion we could
discuss how we messed up putting our sample 6 into well 8 and it flowed over
into well 9 and kind of messed up our gel a little. But we were still able to
get conformation from running the gel and roughly matched our first gel we ran which
was a lot cleaner looking and precise. In
addition, our second gel just seemed to not have ran right for some reason. I am
not sure exactly weather we had some sort of additional contamination or
crossing of our proteins but the bands seemed large and very bright and had
some in places we weren’t expecting to see.
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