RE: ProtSeq

Robert Moritz (Robert.Moritz@ludwig.edu.au)
Sat, 31 Jan 1998 19:27:45 +1100


Dear Paul,
If you know what the sequence of the peptide already is, you
could cleave off the carbohydrate chain with N-Glycosidase F and the
Asparagine residue that is glycosylated will be converted to an Aspartic
acid residue. Should be pretty easy to pick up by sequence analysis
then.

Regards,

Robert Moritz
Joint Protein Structure Laboratory
Ludwig Institute For Cancer Research &
The Walter and Eliza Hall Institute of Medical Research
Royal Melbourne Hospital, Parkville,
Victoria, Australia 3050

> -----Original Message-----
> From: PMotchnik@AOL.com [SMTP:PMotchnik@AOL.com]
> Sent: Saturday, 31 January 1998 5:45
> To: Robert Moritz
> Subject: ProtSeq
>
> Dear ABRFers,
>
> I have a large glycosylated peptide with a high number of serine and
> a few
> aparagine residues. I would like to determine the glycosylated
> residue.
> Would sequencing cleave through a glycosylated site? Since there are
> many
> serine residues making identification of the glycosylated site
> difficult,
> could a carboxypeptidase be used to generate a peptide ending in the
> glycosylated residue? Would a peptidase cleave through a glycosylated
> residue? Any other suggestions would be greatly appreciated. Thanks
> in
> advance.
>
> Paul Motchnik
> XOMA Corp.