Protein Selection

aukbell aukbellNOauSPAM at hotmail.com.invalid
Wed Dec 29 06:56:50 EST 1999


In article <84ar4a$oq4$1 at news.doit.wisc.edu>,
klenchin at facstaff.REMOVE_TO_REPLY.wisc.edu (Dima Klenchin)
wrote:
> In article
> <2180e014.0b9e5e73 at usw-ex0108-061.remarq.com>, aukbell
> <aukbellNOauSPAM at hotmail.com.invalid> wrote:
> :Which methods could be used to produce large amounts
> of X.
> :X is a gene found in a tropical beetle.
> Most certainly it then has to be cloned and expressed
> as
> recombinant protein. Baculovirus system will work for
> sure
> (since it is also insect), but yeasts are worth trying
> as there
> is a non-zero chance that glycosylation in Pichia
> might result
> in active protein.
> :X has theraputic values.
> Wellll........ :-)
> :X is a 70KDa glycoprotein whose active form is a
> trimer.
> :Glycosylation is essential for its activities.
> Glycosylate proteins can be conveniently purified on
> immobilized
> lectin columns. Which one will work can only be found
> empyrically.
> Recombinant protein can be tagged and purified based
> on tag, too.
>         - Dima

If another usefull gene (y) was also found in the same
beetle, how would you modify the method to purify and
culture both genes?

Maybe through the use of restrictive endonucleises??
Which ones??

Y is a 20KDa mono..



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