O-linked glycosylation

MSLADE at RNA.BIO.MQ.EDU.AU MSLADE at RNA.BIO.MQ.EDU.AU
Mon Mar 20 18:16:41 EST 1995


>To:            glycosci at net.bio.net
>From:          R.Lauder at lancaster.ac.uk (Bob Lauder)
>Subject:       Re: O-linked glycosylation
>Date:          20 Mar 1995 13:22:32 GMT
>
>In article <3kc99i$nvt at mserv1.dl.ac.uk>, "Tim Dudgeon" <dudgeon at britbio.co.uk> says:
>>I have ..partially glycosylated with O-liked sugar (there are no N-linked sites in 
>the protein). I wish to seperate the glycosylated form the unglycosylated protein.
>
>>I have tried using ConA-Sepharose (Pharmacia) 
>
>Con-A will almost certainly not bind your O-linked glycan chains. Con-A does have a 
>use for the separation of O-linked from N-linked chains, which it will, in gene
ral, 
>bind.............

>You could try a different approach - if the glycan chains are charged (sulphated ?) 
>then an ion exchange column may be useful. Are the chains capped by Sialic acid ? 
>if so then Sambucus nigra will bind (2-6)-linked Sialic acids. The Lectin for 
>(2-3)-linked Sialic acid, Maccia, has been less sucessful in my hands (columns?).
>

Doesn't this makes the very big assumption that the O-linked glycosylation is 
mammalian?  Other organisms have a big variety of O-linked structures.  Has any one 
worked out the O-linked mannose structures of this yeast?  I would be surprised if an 
any yeast produced sialic acids.  Am I correct in saying that no eukayote simpler than 
a echinoderm (sea urchins) produces sialic acids?

Cheers, Martin Slade
Martin Slade,
School of Biological Sciences,
Macquarie University,
NSW 2109,
Australia
FAX  (61 2) 850 8174
Phone(61 2) 850 8210



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