Different behaviour of glycoprotein in two detection system

johnp at GGPL.ARSUSDA.GOV johnp at GGPL.ARSUSDA.GOV
Fri Jan 5 16:09:29 EST 1996


Dear Giorgio:

There is a good liklihood that the charge isoforms may be due to different 
levels of sialic acid on the glycoprotein, and your sialidase treatment 
should show this.  Less likely, I should think, would be the presence of 
other charged groups on the CHO, such as sulfate.  However, another likely 
possibility is that you may have a charge isoform of the PROTEIN.  You could 
perhaps tell this by removing all glycosylation and rerunning your 2-D gels.  
I think that you are fortunate to find only two spots- our glycoprotein 
(pituitary prolactin) yields many charge and molecular weight isoforms, and 
both appear to be due to different protein isoforms and different types of 
glycosylation.

John Proudman
U.S. Department of Agriculture
Agricultural Research Service
Germplasm and Gamete Physiology Laboratory
Beltsville Agricultural Research Center
Beltsville, Maryland 20705 USA

Phone: 301-504-8094
Fax: 301-504-8546
EMail: JohnP at ggpl.arsusda.gov

>Date: 5-Jan-96 15:40:
>Dear fellow researchers,
>A glycoprotein we exctrated from brains reacts in immunoblot with a
>monoclonal against its peptide moyety, as a 100 kD band.
>Following 2D SDS-PAGE, however, the single band becomes two spots, same
>MW but PI at 4.4 and 5.1, respectively. We think this might e due to
>carbohydrate eterogeneicity and we will perform treatment syalidase
>treatment, as soon as we get the enzyme. Apart from this we had had no
>Ideas and we also have no reference on how to study such cases, so that
>any suggestion would be greatly welcome. Thanks in advance for your
>corteous attention.
>
>Giorgio Spagnol, MD
>Institute of Neurology,
>Statal University, Milan,
>Via F. Sforza 35,  20122 Milan, Italy.
>
>Phone: 02-55190390 W, 02-6570326 H
>FAX:    02- 55190392
>E-MAIL: spagnol at galactica.it
>
>
>
>
>
>



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