I am very curious to know what is the formula of the Fmoc-derivative of
N-acetylglucosamine? The amino group already is substituted with the acetyl
group. Does the compound have the three hydroxy groups protected by Fmoc?
Regards. Leo B.
At 09:36 AM 98/7/30 -0400, you wrote:
>Dear Rich,
>
>The Fmoc derivatives of GlcNAc and GalNAc are commercially available. Lisa
>Mints in our group has used them to make peptides that performed well
>during synthesis, cleavage, MALDI-MS analysis and HPLC. So, you should be
>able to obtain peptides that you need.
>
>Best regards,
>Ruth
>
>
>
>At 02:30 PM 7/29/98 -0800, Richard S. Johnson wrote:
>>
>> Does anyone know where one can obtain synthetic O-GlcNAc peptides? If
>> Gerald Hart is correct and O-GlcNAcylation is as common as
>> phosphorylation it seems reasonable to wonder why no one seems to come
>> across this modification all that frequently. In the days prior to
>> when mass spectrometers were in every other protein chem lab, one can
>> understand why this modification was overlooked. Now that mass
>> spectrometers are as common as vortexers, why don't people stumble
>> across O-GlcNAc more often. A possible explanation, according to
>> Gerald Hart is that O-GlcNAc is largely unstable to electrospray and
>> maldi (including IR MALDI). Does anyone have any experience w/
>> O-GlcNAc peptides or know how to obtain synthetic peptides?
>>
>> Regards, Rich Johnson (rjohnson@immunex.com)
>>
>>
>>______________________________ Reply Separator
>_________________________________
>>Subject: Re: Posttranslational Modifications
>>Author: Ken Mitchelhill <k.mitchelhill@medicine.unimelb.edu.au> at Internet
>>Date: 7/29/98 1:24 PM
>>
>>
>>To: Ken Walsh
>>
>>Ken,
>>
>>In "the other Ken's" original post, he stated the doublet ran "about twice
>>the distance between the phospho and non-phosho forms of either individual
>>species" in isoelectric focussing.
>>
>>Gerald Hart presented his "dynamic glycosylation" data at Lorne this year
>>and we have been looking out for it in some of the regulatory systems we
>>are interested in. I am curious if you, or anyone else out there, knows how
>>GlcNacylation would be expected to affect the isoelectric mobility of a
>>protein?
>>
>>regards....Ken Mitchelhill
>>
>>>Ken
>>>
>>>An interesting possibility for a PTM would be attachment of a single
>>>hexosamine (+161). Gerald Hart has found that specific glycation (with
>>>GlcNac I think) acts to limit phosphorylation.
>>>
>>>Ken
>>>
>>>Kenneth A. Walsh
>>>E.W.Davie/ZymoGenetics Chair of Biochemistry
>>>Box # 357350
>>>University of Washington
>>>Seattle WA 98195
>>>
>>>walsh@u.washington.edu
>>>Phone 206-543-1768
>>>FAX 206-685-9231
>>>
>>>On Mon, 27 Jul 1998, Kenneth Williams wrote:
>>>
>>>> One of our users is working with a kinase that is phosphorylated at a
>>>> single site. In addition, however, the non-phosphorylated (and
>>>> dephosphorylated) kinase migrates as a doublet on isoelectric focussing -
>>>> with the distance between the two (non-phosphorylated) species being
>about
>>>> twice the distance between the phospho and non-phosho forms of either
>>>> individual species. My question is what are the most likely
>>>> post-translational modifications that might give rise to the original
>>>> doublet (assuming one species in not modified and that neiterh is
>>>> phosphorylated).
>>>>
>>>> Thanks!
>>>>
>>>>
>>>>
>>>> Ken Williams, Ph.D.
>>>> Director, HHMI Biopolymer/Keck Laboratory
>>>> Professor (Adjunct) Research
>>>> Molecular Biophysics and Biochemistry
>>>>
>>>>
>>>> Visit the HHMI Biopolymer/Keck Laboratory Web Page at:
>>>>
>>>> http://info.med.yale.edu/wmkeck/
>>>>
>>>>
>>
>>
>>********************************
>>
>>Ken I. Mitchelhill
>>The John Holt Protein Structure Laboratory
>>St. Vincent's Institute of Medical Research
>>41 Victoria Parade
>>Fitzroy 3065 Victoria
>>AUSTRALIA
>>
>>Telephone: 61-3-9288 2480
>>Facsimile: 61-3-9416 2676
>>
>>Email: k.mitchelhill@medicine.unimelb.edu.au
>>
>>Laboratory: http://www.medstv.unimelb.edu.au/WWWDOCS/SVIMRdocs/JHPSL.html
>>ABRF: http://www.abrf.org
>>
>>***********************************
>>
>>
>>
>>
>>
>>
>>
>
>
N. Leo Benoiton
Department of Biochemistry
University of Ottawa
Ottawa, Ontario, Canada K1H 8M5
Tel: 613 562 5800, Ext. 8216
Fax: 613 562 5440
eMail: benoiton@uottawa.ca