John Philo "jphilo*NO SPAM12*" at earthlink.net
Tue Sep 1 19:13:44 EST 1998

You would find very little erythropoietin in kidney tissue--it is a
secreted protein.  Whatever EPO is still inside the cells (mostly in the
Golgi) is probably not completely glycosylated and would therefore have
poor bioactivity.

In principle EPO can be isolated from urine, but there is not much of it
there (this is a very potent hormone).  When this is done is usually
involves hundreds of liters of urine--not much fun! That procedure was
described in a patent by Genetics Institute, and perhaps has also been
published in the normal scientific literature.

The only real way to obtain EPO in therapeutically useful quantities is
to make it recombinantly, and it must be made in cells capable of adding
the glycosylation or it is not active in vivo.

John Philo, Alliance Protein Laboratories

HRF Glaudemans wrote:
> We want to isolate Erytropoëtin out of kidneys. This hormone is used as
> medicin to create more erytrocytes. It's the greatest solution for
> kidney patients.
> All we want to know, is the downstream process to obtain the hormone.
> TXS a lot..............


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