In article <20030323001320.18467.qmail at ww02.hostica.com>,
<pink_flamingo at mexico.com> wrote: > >Q/ You want to prepare a quantity of
a protein from a biological sample. The protein has a MW of about 45kD
and a pI of 6. It binds to the amino acid tyrosine but in the crude
biological sample the protein is already saturdated with tyrosine, and the
protein is unstable below its isoeletric point. Outline a scheme, by
which the protein could be purified by chromatographic means..including
stationary phase, and conditions for elcution etc > >
You might be able to use affinity chromatography if first you
separated the protein from the small tyrosine (although in real life, the
affinity for tyrosine might be too great to allow this). Alternatively,
you could take advantage of the protein's charge at higher pH (since
you're not allowed to use a lower pH).
--
______________________________________________________________________________
Lou Hom >K'93
lhom at ocf.berkeley.eduhttp://www.ocf.berkeley.edu/~lhom/
