Seperation Techniques

Louis Hom lhom at OCF.Berkeley.EDU
Sun Mar 23 01:04:41 EST 2003

In article <20030323001320.18467.qmail at>,
 <pink_flamingo at> 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 	    

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