>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
>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
School of Biological Sciences,
FAX (61 2) 850 8174
Phone(61 2) 850 8210