Hi everyone. I´m working with a lipid binding protein
that shows in SDS-PAGE, under non-reducing and
reducing conditions, a ladder-type pattern of
subunits. Some lines of evidence indicates to me that
the lipid-protein motifs are organized in a hydrophic
core/polar outer shield, similar to that described for
animal serum lipoproteins. Moreover, some previous
observations has shown that this structural
organization is not significantly altered even in the
presence of 6M urea.
Then my specific question is: if the native protein is
treated in order to be analized by denaturing PAGE
(non-red. or red.), (that is heated at 105 degrees for
5 min in the presence of SDS) and a band corresponding
to a particular subunit is scissed from the gel and
the protein is then recovered by electroelution, ¿is
it possible that some lipids could still be associated
to the protein? If its true, ¿are they binded in a
negligible or significantly amount? ¿or are all the
lipidic components removed during heating in the
presence of detergent? ¿is it possible that the lipids
could not migrate during electrophoresis, so they stay
at the wells on the stacking gel? I am sorry that i
couldn´t make a shorter exposition, but i´ll be very
gratefully. It´s a recent idea that come to my mind
and i could not get a confident answer. Thanks in
advance. G. Obal

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